ES2759980T3 - Péptidos para el manejo de la lactación - Google Patents
Péptidos para el manejo de la lactación Download PDFInfo
- Publication number
- ES2759980T3 ES2759980T3 ES13764905T ES13764905T ES2759980T3 ES 2759980 T3 ES2759980 T3 ES 2759980T3 ES 13764905 T ES13764905 T ES 13764905T ES 13764905 T ES13764905 T ES 13764905T ES 2759980 T3 ES2759980 T3 ES 2759980T3
- Authority
- ES
- Spain
- Prior art keywords
- peptide
- synthetic
- pharmaceutical composition
- amino acid
- ser
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Active
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 126
- 230000006651 lactation Effects 0.000 title claims description 22
- 102000004196 processed proteins & peptides Human genes 0.000 title description 57
- 150000001413 amino acids Chemical class 0.000 claims abstract description 32
- 230000000903 blocking effect Effects 0.000 claims abstract description 9
- 125000000539 amino acid group Chemical group 0.000 claims abstract description 8
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract 5
- 235000013336 milk Nutrition 0.000 claims description 65
- 239000008267 milk Substances 0.000 claims description 65
- 210000004080 milk Anatomy 0.000 claims description 65
- 239000008194 pharmaceutical composition Substances 0.000 claims description 49
- 210000005075 mammary gland Anatomy 0.000 claims description 37
- 238000004519 manufacturing process Methods 0.000 claims description 29
- 239000000203 mixture Substances 0.000 claims description 24
- 241001465754 Metazoa Species 0.000 claims description 22
- 238000011282 treatment Methods 0.000 claims description 17
- 241000124008 Mammalia Species 0.000 claims description 14
- 230000001939 inductive effect Effects 0.000 claims description 11
- 208000015181 infectious disease Diseases 0.000 claims description 10
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 8
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims description 8
- 239000004472 Lysine Substances 0.000 claims description 8
- 230000002085 persistent effect Effects 0.000 claims description 8
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 claims description 7
- 150000001408 amides Chemical class 0.000 claims description 7
- 230000001052 transient effect Effects 0.000 claims description 6
- 210000004899 c-terminal region Anatomy 0.000 claims description 5
- 239000004475 Arginine Substances 0.000 claims description 4
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 claims description 4
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 claims description 4
- 230000000844 anti-bacterial effect Effects 0.000 claims description 4
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims description 4
- 239000003085 diluting agent Substances 0.000 claims description 4
- 239000000839 emulsion Substances 0.000 claims description 4
- 150000002148 esters Chemical class 0.000 claims description 4
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 claims description 4
- 239000002955 immunomodulating agent Substances 0.000 claims description 4
- 230000002584 immunomodulator Effects 0.000 claims description 4
- 229940121354 immunomodulator Drugs 0.000 claims description 4
- 238000007911 parenteral administration Methods 0.000 claims description 4
- 239000003242 anti bacterial agent Substances 0.000 claims description 3
- 239000003899 bactericide agent Substances 0.000 claims description 3
- 239000006071 cream Substances 0.000 claims description 3
- 239000000499 gel Substances 0.000 claims description 3
- 239000002674 ointment Substances 0.000 claims description 3
- 230000003637 steroidlike Effects 0.000 claims description 3
- 238000011200 topical administration Methods 0.000 claims description 3
- 230000002906 microbiologic effect Effects 0.000 claims description 2
- 229940088710 antibiotic agent Drugs 0.000 claims 1
- 239000004599 antimicrobial Substances 0.000 claims 1
- 239000000041 non-steroidal anti-inflammatory agent Substances 0.000 claims 1
- 229940021182 non-steroidal anti-inflammatory drug Drugs 0.000 claims 1
- 230000002265 prevention Effects 0.000 claims 1
- 239000002294 steroidal antiinflammatory agent Substances 0.000 claims 1
- 229960005486 vaccine Drugs 0.000 claims 1
- 238000000034 method Methods 0.000 description 38
- 208000004396 mastitis Diseases 0.000 description 31
- 241000283690 Bos taurus Species 0.000 description 30
- 102000011632 Caseins Human genes 0.000 description 26
- 108010076119 Caseins Proteins 0.000 description 26
- 210000000481 breast Anatomy 0.000 description 24
- 239000005018 casein Substances 0.000 description 23
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 22
- 235000021240 caseins Nutrition 0.000 description 22
- 230000008569 process Effects 0.000 description 18
- 239000000243 solution Substances 0.000 description 18
- 230000028327 secretion Effects 0.000 description 12
- 230000000694 effects Effects 0.000 description 11
- 210000002445 nipple Anatomy 0.000 description 11
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 10
- 239000008101 lactose Substances 0.000 description 10
- 235000013365 dairy product Nutrition 0.000 description 9
- 238000001802 infusion Methods 0.000 description 9
- 244000144980 herd Species 0.000 description 8
- 108010001441 Phosphopeptides Proteins 0.000 description 7
- 230000006698 induction Effects 0.000 description 7
- BZQFBWGGLXLEPQ-REOHCLBHSA-N phosphoserine Chemical group OC(=O)[C@@H](N)COP(O)(O)=O BZQFBWGGLXLEPQ-REOHCLBHSA-N 0.000 description 7
- 241000283707 Capra Species 0.000 description 6
- YSZNURNVYFUEHC-BQBZGAKWSA-N Lys-Ser Chemical compound NCCCC[C@H](N)C(=O)N[C@@H](CO)C(O)=O YSZNURNVYFUEHC-BQBZGAKWSA-N 0.000 description 6
- DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 230000007423 decrease Effects 0.000 description 6
- 238000001035 drying Methods 0.000 description 6
- 238000002347 injection Methods 0.000 description 6
- 239000007924 injection Substances 0.000 description 6
- 238000005259 measurement Methods 0.000 description 6
- 238000003786 synthesis reaction Methods 0.000 description 6
- YDDDRTIPNTWGIG-SRVKXCTJSA-N Lys-Lys-Ser Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CO)C(O)=O YDDDRTIPNTWGIG-SRVKXCTJSA-N 0.000 description 5
- 230000015572 biosynthetic process Effects 0.000 description 5
- 230000035611 feeding Effects 0.000 description 5
- 230000036541 health Effects 0.000 description 5
- 125000006239 protecting group Chemical group 0.000 description 5
- 239000007790 solid phase Substances 0.000 description 5
- QEVHRUUCFGRFIF-UHFFFAOYSA-N 6,18-dimethoxy-17-[oxo-(3,4,5-trimethoxyphenyl)methoxy]-1,3,11,12,14,15,16,17,18,19,20,21-dodecahydroyohimban-19-carboxylic acid methyl ester Chemical compound C1C2CN3CCC(C4=CC=C(OC)C=C4N4)=C4C3CC2C(C(=O)OC)C(OC)C1OC(=O)C1=CC(OC)=C(OC)C(OC)=C1 QEVHRUUCFGRFIF-UHFFFAOYSA-N 0.000 description 4
- 101100533283 Dictyostelium discoideum serp gene Proteins 0.000 description 4
- 125000001797 benzyl group Chemical group [H]C1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])* 0.000 description 4
- 230000003115 biocidal effect Effects 0.000 description 4
- 239000002775 capsule Substances 0.000 description 4
- 239000003814 drug Substances 0.000 description 4
- 229940079593 drug Drugs 0.000 description 4
- 125000001495 ethyl group Chemical group [H]C([H])([H])C([H])([H])* 0.000 description 4
- 235000013305 food Nutrition 0.000 description 4
- 210000004907 gland Anatomy 0.000 description 4
- 230000007062 hydrolysis Effects 0.000 description 4
- 238000006460 hydrolysis reaction Methods 0.000 description 4
- 230000000474 nursing effect Effects 0.000 description 4
- 238000001139 pH measurement Methods 0.000 description 4
- 238000010647 peptide synthesis reaction Methods 0.000 description 4
- 230000035935 pregnancy Effects 0.000 description 4
- 229940080237 sodium caseinate Drugs 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 210000001082 somatic cell Anatomy 0.000 description 4
- 230000008961 swelling Effects 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- 230000000699 topical effect Effects 0.000 description 4
- BZQFBWGGLXLEPQ-UHFFFAOYSA-N O-phosphoryl-L-serine Natural products OC(=O)C(N)COP(O)(O)=O BZQFBWGGLXLEPQ-UHFFFAOYSA-N 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 102000004142 Trypsin Human genes 0.000 description 3
- 108090000631 Trypsin Proteins 0.000 description 3
- 230000001154 acute effect Effects 0.000 description 3
- 230000006907 apoptotic process Effects 0.000 description 3
- 239000000872 buffer Substances 0.000 description 3
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 3
- 210000004027 cell Anatomy 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- 229950006137 dexfosfoserine Drugs 0.000 description 3
- 238000000605 extraction Methods 0.000 description 3
- 238000009472 formulation Methods 0.000 description 3
- 235000020256 human milk Nutrition 0.000 description 3
- 210000004251 human milk Anatomy 0.000 description 3
- 230000000670 limiting effect Effects 0.000 description 3
- 238000007726 management method Methods 0.000 description 3
- 230000008520 organization Effects 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 235000018102 proteins Nutrition 0.000 description 3
- 102000004169 proteins and genes Human genes 0.000 description 3
- 108090000623 proteins and genes Proteins 0.000 description 3
- 230000002441 reversible effect Effects 0.000 description 3
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 208000024891 symptom Diseases 0.000 description 3
- 210000001519 tissue Anatomy 0.000 description 3
- 239000012588 trypsin Substances 0.000 description 3
- 125000004178 (C1-C4) alkyl group Chemical group 0.000 description 2
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 2
- 102000002322 Egg Proteins Human genes 0.000 description 2
- 108010000912 Egg Proteins Proteins 0.000 description 2
- 241000233866 Fungi Species 0.000 description 2
- 241000282412 Homo Species 0.000 description 2
- 206010061218 Inflammation Diseases 0.000 description 2
- 206010028980 Neoplasm Diseases 0.000 description 2
- 241001494479 Pecora Species 0.000 description 2
- 101800005149 Peptide B Proteins 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical group OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 2
- 241000282887 Suidae Species 0.000 description 2
- 102000000591 Tight Junction Proteins Human genes 0.000 description 2
- 108010002321 Tight Junction Proteins Proteins 0.000 description 2
- 230000005856 abnormality Effects 0.000 description 2
- 125000001931 aliphatic group Chemical group 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 238000011861 anti-inflammatory therapy Methods 0.000 description 2
- 238000011203 antimicrobial therapy Methods 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 230000004071 biological effect Effects 0.000 description 2
- 235000013345 egg yolk Nutrition 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 230000007717 exclusion Effects 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 239000012634 fragment Substances 0.000 description 2
- 239000011521 glass Substances 0.000 description 2
- 230000007407 health benefit Effects 0.000 description 2
- 125000000623 heterocyclic group Chemical group 0.000 description 2
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 2
- 230000002434 immunopotentiative effect Effects 0.000 description 2
- 230000004054 inflammatory process Effects 0.000 description 2
- 238000002483 medication Methods 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 2
- 230000009826 neoplastic cell growth Effects 0.000 description 2
- 229910052757 nitrogen Inorganic materials 0.000 description 2
- 239000003960 organic solvent Substances 0.000 description 2
- 125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 description 2
- 230000026731 phosphorylation Effects 0.000 description 2
- 238000006366 phosphorylation reaction Methods 0.000 description 2
- 239000013641 positive control Substances 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 238000005070 sampling Methods 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 235000021055 solid food Nutrition 0.000 description 2
- 238000010532 solid phase synthesis reaction Methods 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 238000013268 sustained release Methods 0.000 description 2
- 239000012730 sustained-release form Substances 0.000 description 2
- 230000009885 systemic effect Effects 0.000 description 2
- 238000002560 therapeutic procedure Methods 0.000 description 2
- 210000001578 tight junction Anatomy 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- 206010000234 Abortion spontaneous Diseases 0.000 description 1
- 208000030090 Acute Disease Diseases 0.000 description 1
- 235000002198 Annona diversifolia Nutrition 0.000 description 1
- 238000012371 Aseptic Filling Methods 0.000 description 1
- 208000031462 Bovine Mastitis Diseases 0.000 description 1
- 206010006223 Breast discharge Diseases 0.000 description 1
- 101100294102 Caenorhabditis elegans nhr-2 gene Chemical group 0.000 description 1
- 241000282832 Camelidae Species 0.000 description 1
- 241000282472 Canis lupus familiaris Species 0.000 description 1
- 102000016938 Catalase Human genes 0.000 description 1
- 108010053835 Catalase Proteins 0.000 description 1
- 108091006146 Channels Proteins 0.000 description 1
- 208000017667 Chronic Disease Diseases 0.000 description 1
- 241000195493 Cryptophyta Species 0.000 description 1
- 241001315286 Damon Species 0.000 description 1
- 108010016626 Dipeptides Proteins 0.000 description 1
- 206010013082 Discomfort Diseases 0.000 description 1
- 241000283086 Equidae Species 0.000 description 1
- 241000283074 Equus asinus Species 0.000 description 1
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 1
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- 208000027472 Galactosemias Diseases 0.000 description 1
- 239000012981 Hank's balanced salt solution Substances 0.000 description 1
- 241000725303 Human immunodeficiency virus Species 0.000 description 1
- 241000282838 Lama Species 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 239000001888 Peptone Substances 0.000 description 1
- 208000037581 Persistent Infection Diseases 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 102000004257 Potassium Channel Human genes 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 206010037660 Pyrexia Diseases 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- NINIDFKCEFEMDL-UHFFFAOYSA-N Sulfur Chemical group [S] NINIDFKCEFEMDL-UHFFFAOYSA-N 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 208000027418 Wounds and injury Diseases 0.000 description 1
- 230000002159 abnormal effect Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 208000036981 active tuberculosis Diseases 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- XAGFODPZIPBFFR-UHFFFAOYSA-N aluminium Chemical compound [Al] XAGFODPZIPBFFR-UHFFFAOYSA-N 0.000 description 1
- 229910052782 aluminium Inorganic materials 0.000 description 1
- 125000003368 amide group Chemical group 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 230000004596 appetite loss Effects 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical group [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 1
- 230000008952 bacterial invasion Effects 0.000 description 1
- 210000002469 basement membrane Anatomy 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 229960003168 bronopol Drugs 0.000 description 1
- 238000004364 calculation method Methods 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 210000000991 chicken egg Anatomy 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 238000009833 condensation Methods 0.000 description 1
- 230000005494 condensation Effects 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 230000002596 correlated effect Effects 0.000 description 1
- 230000000875 corresponding effect Effects 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000034994 death Effects 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000000593 degrading effect Effects 0.000 description 1
- 238000010511 deprotection reaction Methods 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 235000005911 diet Nutrition 0.000 description 1
- 230000037213 diet Effects 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 239000013583 drug formulation Substances 0.000 description 1
- 210000002969 egg yolk Anatomy 0.000 description 1
- 210000002889 endothelial cell Anatomy 0.000 description 1
- 210000002744 extracellular matrix Anatomy 0.000 description 1
- 235000021050 feed intake Nutrition 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 235000013350 formula milk Nutrition 0.000 description 1
- 235000015203 fruit juice Nutrition 0.000 description 1
- 230000000762 glandular Effects 0.000 description 1
- 239000003163 gonadal steroid hormone Substances 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 125000005842 heteroatom Chemical group 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 230000036512 infertility Effects 0.000 description 1
- 230000028709 inflammatory response Effects 0.000 description 1
- 208000014674 injury Diseases 0.000 description 1
- 239000002198 insoluble material Substances 0.000 description 1
- 230000007794 irritation Effects 0.000 description 1
- 125000001449 isopropyl group Chemical group [H]C([H])([H])C([H])(*)C([H])([H])[H] 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 235000021266 loss of appetite Nutrition 0.000 description 1
- 208000019017 loss of appetite Diseases 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 210000004379 membrane Anatomy 0.000 description 1
- 125000000956 methoxy group Chemical group [H]C([H])([H])O* 0.000 description 1
- 239000000693 micelle Substances 0.000 description 1
- 230000003278 mimic effect Effects 0.000 description 1
- 208000015994 miscarriage Diseases 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- -1 morpholino, thiomorpholino Chemical group 0.000 description 1
- 125000004108 n-butyl group Chemical group [H]C([H])([H])C([H])([H])C([H])([H])C([H])([H])* 0.000 description 1
- 125000004123 n-propyl group Chemical group [H]C([H])([H])C([H])([H])C([H])([H])* 0.000 description 1
- IJGRMHOSHXDMSA-UHFFFAOYSA-N nitrogen Substances N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 1
- 125000004433 nitrogen atom Chemical group N* 0.000 description 1
- QJGQUHMNIGDVPM-UHFFFAOYSA-N nitrogen group Chemical group [N] QJGQUHMNIGDVPM-UHFFFAOYSA-N 0.000 description 1
- 230000001937 non-anti-biotic effect Effects 0.000 description 1
- 230000036542 oxidative stress Effects 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 239000001301 oxygen Chemical group 0.000 description 1
- 244000045947 parasite Species 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 125000004193 piperazinyl group Chemical group 0.000 description 1
- 125000003386 piperidinyl group Chemical group 0.000 description 1
- 229940127126 plasminogen activator Drugs 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 108020001213 potassium channel Proteins 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000004262 preparative liquid chromatography Methods 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000002335 preservative effect Effects 0.000 description 1
- 125000000719 pyrrolidinyl group Chemical group 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 230000001172 regenerating effect Effects 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 125000002914 sec-butyl group Chemical group [H]C([H])([H])C([H])([H])C([H])(*)C([H])([H])[H] 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 208000026777 severe mastitis Diseases 0.000 description 1
- 238000003307 slaughter Methods 0.000 description 1
- 208000000995 spontaneous abortion Diseases 0.000 description 1
- 238000013112 stability test Methods 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 125000003107 substituted aryl group Chemical group 0.000 description 1
- 229910052717 sulfur Chemical group 0.000 description 1
- 239000011593 sulfur Chemical group 0.000 description 1
- 230000001360 synchronised effect Effects 0.000 description 1
- 238000007910 systemic administration Methods 0.000 description 1
- 125000000999 tert-butyl group Chemical group [H]C([H])([H])C(*)(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 238000001269 time-of-flight mass spectrometry Methods 0.000 description 1
- 230000007838 tissue remodeling Effects 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 108700012359 toxins Proteins 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000007704 transition Effects 0.000 description 1
- 230000001960 triggered effect Effects 0.000 description 1
- 201000008827 tuberculosis Diseases 0.000 description 1
- 238000002255 vaccination Methods 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/04—Peptides having up to 20 amino acids in a fully defined sequence; Derivatives thereof
- A61K38/07—Tetrapeptides
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/04—Peptides having up to 20 amino acids in a fully defined sequence; Derivatives thereof
- A61K38/08—Peptides having 5 to 11 amino acids
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K45/00—Medicinal preparations containing active ingredients not provided for in groups A61K31/00 - A61K41/00
- A61K45/06—Mixtures of active ingredients without chemical characterisation, e.g. antiphlogistics and cardiaca
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P15/00—Drugs for genital or sexual disorders; Contraceptives
- A61P15/14—Drugs for genital or sexual disorders; Contraceptives for lactation disorders, e.g. galactorrhoea
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4732—Casein
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/10—Tetrapeptides
- C07K5/1019—Tetrapeptides with the first amino acid being basic
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/1703—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- A61K38/1709—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Organic Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Pharmacology & Pharmacy (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Gastroenterology & Hepatology (AREA)
- Epidemiology (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Molecular Biology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Immunology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Zoology (AREA)
- Toxicology (AREA)
- Pain & Pain Management (AREA)
- Reproductive Health (AREA)
- Communicable Diseases (AREA)
- Endocrinology (AREA)
- Pregnancy & Childbirth (AREA)
- Gynecology & Obstetrics (AREA)
- Rheumatology (AREA)
- Oncology (AREA)
- Marine Sciences & Fisheries (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201261612410P | 2012-03-19 | 2012-03-19 | |
| PCT/IL2013/050214 WO2013140388A1 (en) | 2012-03-19 | 2013-03-08 | Peptides for management of lactation |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2759980T3 true ES2759980T3 (es) | 2020-05-12 |
Family
ID=49221927
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES13764905T Active ES2759980T3 (es) | 2012-03-19 | 2013-03-08 | Péptidos para el manejo de la lactación |
Country Status (11)
| Country | Link |
|---|---|
| US (1) | US9487557B2 (enExample) |
| EP (1) | EP2828281B1 (enExample) |
| JP (1) | JP6426599B2 (enExample) |
| CN (1) | CN104321336B (enExample) |
| AU (1) | AU2013236975B2 (enExample) |
| BR (1) | BR112014023087A8 (enExample) |
| CA (1) | CA2867557C (enExample) |
| ES (1) | ES2759980T3 (enExample) |
| IL (1) | IL234574B (enExample) |
| IN (1) | IN2014DN08610A (enExample) |
| WO (1) | WO2013140388A1 (enExample) |
Families Citing this family (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| KR102022118B1 (ko) * | 2019-01-07 | 2019-09-18 | 주식회사 아스트로젠 | 중추신경계 질환의 예방 또는 치료용 세린 유도체 화합물 |
| CN111632128B (zh) * | 2019-02-14 | 2022-07-05 | 三凡生技研发股份有限公司 | 短链胜肽组合物在预防或治疗干眼症的应用 |
| AU2020394498A1 (en) | 2019-11-28 | 2022-06-09 | Boehringer Ingelheim Vetmedica Gmbh | Use of SGLT-2 inhibitors in the drying-off of non-human mammals |
| BR112023022624A2 (pt) * | 2021-04-28 | 2024-01-16 | Mileutis Ltd | Composições e métodos para modular distúrbios e condições mamárias |
Family Cites Families (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6391849B1 (en) | 1999-11-19 | 2002-05-21 | Agricultural Research Organization, The Volcani Center | Method and pharmaceutical composition for disrupting lactation in a mammary gland and for treating and preventing mastitis |
| CN1496368A (zh) | 2001-03-09 | 2004-05-12 | 明治制果株式会社 | 免疫增强剂 |
| CN101247721B (zh) * | 2005-05-02 | 2016-08-03 | 米勒尤迪斯公司 | 包括酪蛋白衍生肽的药物组合物及其使用方法 |
| ES2400511T3 (es) * | 2005-05-02 | 2013-04-10 | Mileutis Ltd. | Composiciones farmacéuticas que comprenden péptidos derivados de la caseina y métodos para el uso de las mismas |
| WO2009023270A2 (en) * | 2007-08-15 | 2009-02-19 | Amunix, Inc. | Compositions and methods for modifying properties of biologically active polypeptides |
-
2013
- 2013-03-08 ES ES13764905T patent/ES2759980T3/es active Active
- 2013-03-08 CA CA2867557A patent/CA2867557C/en active Active
- 2013-03-08 US US14/384,395 patent/US9487557B2/en active Active
- 2013-03-08 JP JP2015501047A patent/JP6426599B2/ja active Active
- 2013-03-08 CN CN201380025974.9A patent/CN104321336B/zh active Active
- 2013-03-08 BR BR112014023087A patent/BR112014023087A8/pt not_active Application Discontinuation
- 2013-03-08 AU AU2013236975A patent/AU2013236975B2/en active Active
- 2013-03-08 IN IN8610DEN2014 patent/IN2014DN08610A/en unknown
- 2013-03-08 WO PCT/IL2013/050214 patent/WO2013140388A1/en not_active Ceased
- 2013-03-08 EP EP13764905.9A patent/EP2828281B1/en active Active
-
2014
- 2014-09-10 IL IL234574A patent/IL234574B/en active IP Right Grant
Also Published As
| Publication number | Publication date |
|---|---|
| CA2867557C (en) | 2020-03-10 |
| US20150093400A1 (en) | 2015-04-02 |
| IN2014DN08610A (enExample) | 2015-05-22 |
| EP2828281A4 (en) | 2015-11-11 |
| BR112014023087A2 (pt) | 2017-06-20 |
| EP2828281A1 (en) | 2015-01-28 |
| BR112014023087A8 (pt) | 2018-01-16 |
| CN104321336B (zh) | 2021-08-06 |
| US9487557B2 (en) | 2016-11-08 |
| AU2013236975A1 (en) | 2014-10-23 |
| IL234574B (en) | 2020-09-30 |
| JP2015516377A (ja) | 2015-06-11 |
| CN104321336A (zh) | 2015-01-28 |
| EP2828281B1 (en) | 2019-09-18 |
| JP6426599B2 (ja) | 2018-11-21 |
| WO2013140388A1 (en) | 2013-09-26 |
| AU2013236975B2 (en) | 2017-10-19 |
| CA2867557A1 (en) | 2013-09-26 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US8338363B2 (en) | Pharmaceutical compositions comprising casein derived peptides and methods of use thereof | |
| ES2249207T3 (es) | Agente de supresion de la resorcion osea. | |
| ES2759980T3 (es) | Péptidos para el manejo de la lactación | |
| PT88626B (pt) | Processo para a preparacao de um factor de crescimento polipeptidico proveniente de leite | |
| ES2738287T3 (es) | Inhibidor de la formación de trampas extracelulares en leucocitos | |
| ES2681894T3 (es) | Uso de una membrana de célula vegetal para el tratamiento de la obesidad | |
| US20090305947A1 (en) | Livestock management for improved reproductive efficiency | |
| ES2887086T3 (es) | Procedimiento para producir yema de huevo con alto contenido de af-16 | |
| JP2008540399A5 (enExample) | ||
| CN101247721B (zh) | 包括酪蛋白衍生肽的药物组合物及其使用方法 | |
| RU2264229C2 (ru) | Препарат секреторного иммуноглобулина а, обладающий противовирусным и антибактериальным действием | |
| AU2012200889B2 (en) | Pharmaceutical compositions comprising casein derived peptides and methods of use thereof | |
| BR112020007037A2 (pt) | variantes de g-csf porcino e seus usos | |
| WO2025209335A1 (zh) | 包含谷氨酰胺源物质的组合物及其用途 | |
| IL222487A (en) | Casein-derived peptides and methods for using them to increase milk yield | |
| IL222486A (en) | Casein-derived peptides and methods for using them to enhance milk cleanliness | |
| JPWO2007037099A1 (ja) | 乳房炎の治療剤 | |
| WO2009148294A1 (es) | Extracto de piel de rana catesbeiana, compuesto y método para tratar la mastitis en bovinos |