NO833633L - Nye forbindelser for bruk i antibakteriell terapi - Google Patents
Nye forbindelser for bruk i antibakteriell terapiInfo
- Publication number
- NO833633L NO833633L NO833633A NO833633A NO833633L NO 833633 L NO833633 L NO 833633L NO 833633 A NO833633 A NO 833633A NO 833633 A NO833633 A NO 833633A NO 833633 L NO833633 L NO 833633L
- Authority
- NO
- Norway
- Prior art keywords
- dab
- thr
- leucine
- polymyxin
- threonine
- Prior art date
Links
- 230000000844 anti-bacterial effect Effects 0.000 title description 5
- 238000002560 therapeutic procedure Methods 0.000 title description 2
- PYHYGIPVYYRJHU-LPGHPFMSSA-N (2s,3r)-2-amino-n-[(2s)-4-amino-1-oxo-1-[[(3s,6s,9s,12s,15s,18s,21s)-6,9,18-tris(2-aminoethyl)-15-benzyl-3-[(1r)-1-hydroxyethyl]-12-(2-methylpropyl)-2,5,8,11,14,17,20-heptaoxo-1,4,7,10,13,16,19-heptazacyclotricos-21-yl]amino]butan-2-yl]-3-hydroxybutanamid Polymers N1C(=O)[C@H](CCN)NC(=O)[C@@H](NC(=O)[C@H](CCN)NC(=O)[C@@H](N)[C@@H](C)O)CCNC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCN)NC(=O)[C@H](CCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H]1CC1=CC=CC=C1 PYHYGIPVYYRJHU-LPGHPFMSSA-N 0.000 claims description 55
- 108700026839 polymyxin B nonapeptide Proteins 0.000 claims description 54
- 150000001875 compounds Chemical class 0.000 claims description 30
- 241000894006 Bacteria Species 0.000 claims description 29
- 108010078777 Colistin Proteins 0.000 claims description 27
- XDJYMJULXQKGMM-UHFFFAOYSA-N polymyxin E1 Natural products CCC(C)CCCCC(=O)NC(CCN)C(=O)NC(C(C)O)C(=O)NC(CCN)C(=O)NC1CCNC(=O)C(C(C)O)NC(=O)C(CCN)NC(=O)C(CCN)NC(=O)C(CC(C)C)NC(=O)C(CC(C)C)NC(=O)C(CCN)NC1=O XDJYMJULXQKGMM-UHFFFAOYSA-N 0.000 claims description 27
- JORAUNFTUVJTNG-BSTBCYLQSA-N n-[(2s)-4-amino-1-[[(2s,3r)-1-[[(2s)-4-amino-1-oxo-1-[[(3s,6s,9s,12s,15r,18s,21s)-6,9,18-tris(2-aminoethyl)-3-[(1r)-1-hydroxyethyl]-12,15-bis(2-methylpropyl)-2,5,8,11,14,17,20-heptaoxo-1,4,7,10,13,16,19-heptazacyclotricos-21-yl]amino]butan-2-yl]amino]-3-h Polymers CC(C)CCCCC(=O)N[C@@H](CCN)C(=O)N[C@H]([C@@H](C)O)CN[C@@H](CCN)C(=O)N[C@H]1CCNC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCN)NC(=O)[C@H](CCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](CC(C)C)NC(=O)[C@H](CCN)NC1=O.CCC(C)CCCCC(=O)N[C@@H](CCN)C(=O)N[C@H]([C@@H](C)O)CN[C@@H](CCN)C(=O)N[C@H]1CCNC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCN)NC(=O)[C@H](CCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](CC(C)C)NC(=O)[C@H](CCN)NC1=O JORAUNFTUVJTNG-BSTBCYLQSA-N 0.000 claims description 26
- 239000003242 anti bacterial agent Substances 0.000 claims description 25
- 238000000034 method Methods 0.000 claims description 22
- 230000000295 complement effect Effects 0.000 claims description 19
- YKQOSKADJPQZHB-YNWHQGOSSA-N n-[(2s)-4-amino-1-[[(2s,3r)-1-[[(2s)-4-amino-1-oxo-1-[[(3s,6s,9s,12s,15r,18s,21s)-6,9,18-tris(2-aminoethyl)-3-[(1s)-1-hydroxyethyl]-12,15-bis(2-methylpropyl)-2,5,8,11,14,17,20-heptaoxo-1,4,7,10,13,16,19-heptazacyclotricos-21-yl]amino]butan-2-yl]amino]-3-h Polymers CCC(C)CCCC(=O)N[C@@H](CCN)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCN)C(=O)N[C@H]1CCNC(=O)[C@H]([C@H](C)O)NC(=O)[C@H](CCN)NC(=O)[C@H](CCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](CC(C)C)NC(=O)[C@H](CCN)NC1=O YKQOSKADJPQZHB-YNWHQGOSSA-N 0.000 claims description 19
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 claims description 18
- 239000004473 Threonine Substances 0.000 claims description 18
- 239000004365 Protease Substances 0.000 claims description 17
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 claims description 15
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 claims description 15
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 claims description 14
- 108010093965 Polymyxin B Proteins 0.000 claims description 13
- 108010040201 Polymyxins Proteins 0.000 claims description 12
- 239000002253 acid Substances 0.000 claims description 10
- 125000002252 acyl group Chemical group 0.000 claims description 10
- 125000000341 threoninyl group Chemical group [H]OC([H])(C([H])([H])[H])C([H])(N([H])[H])C(*)=O 0.000 claims description 10
- BLCJBICVQSYOIF-UHFFFAOYSA-N 2,2-diaminobutanoic acid Chemical group CCC(N)(N)C(O)=O BLCJBICVQSYOIF-UHFFFAOYSA-N 0.000 claims description 9
- 108090000270 Ficain Proteins 0.000 claims description 9
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 claims description 9
- 235000019836 ficin Nutrition 0.000 claims description 9
- POTUGHMKJGOKRI-UHFFFAOYSA-N ficin Chemical compound FI=CI=N POTUGHMKJGOKRI-UHFFFAOYSA-N 0.000 claims description 9
- 229920000024 polymyxin B Polymers 0.000 claims description 9
- 229960005266 polymyxin b Drugs 0.000 claims description 9
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 claims description 8
- ROHFNLRQFUQHCH-RXMQYKEDSA-N D-leucine Chemical compound CC(C)C[C@@H](N)C(O)=O ROHFNLRQFUQHCH-RXMQYKEDSA-N 0.000 claims description 7
- 229930182819 D-leucine Natural products 0.000 claims description 6
- COLNVLDHVKWLRT-MRVPVSSYSA-N D-phenylalanine Chemical compound OC(=O)[C@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-MRVPVSSYSA-N 0.000 claims description 6
- 229930182832 D-phenylalanine Natural products 0.000 claims description 6
- MUBZPKHOEPUJKR-UHFFFAOYSA-N Oxalic acid Chemical compound OC(=O)C(O)=O MUBZPKHOEPUJKR-UHFFFAOYSA-N 0.000 claims description 6
- 108090000526 Papain Proteins 0.000 claims description 6
- 238000004519 manufacturing process Methods 0.000 claims description 6
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 claims description 6
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 claims description 5
- 206010070834 Sensitisation Diseases 0.000 claims description 5
- 125000004432 carbon atom Chemical group C* 0.000 claims description 5
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 claims description 5
- 229960000310 isoleucine Drugs 0.000 claims description 5
- 239000000203 mixture Substances 0.000 claims description 5
- 229940055729 papain Drugs 0.000 claims description 5
- 235000019834 papain Nutrition 0.000 claims description 5
- 150000003839 salts Chemical class 0.000 claims description 5
- 230000008313 sensitization Effects 0.000 claims description 5
- 230000001235 sensitizing effect Effects 0.000 claims description 5
- OAKJQQAXSVQMHS-UHFFFAOYSA-N Hydrazine Chemical compound NN OAKJQQAXSVQMHS-UHFFFAOYSA-N 0.000 claims description 4
- 230000009471 action Effects 0.000 claims description 4
- 108010002696 circulin Proteins 0.000 claims description 4
- YLHJFOAQDDQFIU-UHFFFAOYSA-N circulin Chemical compound CCC(C)C1NC(=O)C(CC(C)C)NC(=O)C(CCN)NC(=O)C(NC(=O)C(CCN)NC(=O)C(NC(=O)C(CCN)NC=O)C(C)O)CCNC(=O)C(C(C)O)NC(=O)C(CCN)NC(=O)C(CCN)NC1=O YLHJFOAQDDQFIU-UHFFFAOYSA-N 0.000 claims description 4
- HEDADCOWECPKFY-UHFFFAOYSA-N octapeptin Chemical compound CCC(C)CCCCC(O)CC(=O)NC(CCN)C(=O)NC1CCNC(=O)C(CC(C)C)NC(=O)C(CCN)NC(=O)C(CCN)NC(=O)C(CC(C)C)NC(=O)C(CC(C)C)NC(=O)C(CCN)NC1=O HEDADCOWECPKFY-UHFFFAOYSA-N 0.000 claims description 4
- 125000001424 substituent group Chemical group 0.000 claims description 4
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 claims description 3
- 108010004032 Bromelains Proteins 0.000 claims description 3
- 108090000790 Enzymes Proteins 0.000 claims description 3
- 102000004190 Enzymes Human genes 0.000 claims description 3
- 235000019835 bromelain Nutrition 0.000 claims description 3
- 108700031796 cyclo(diaminobutyryl-diaminobutyryl-phenylalanyl-leucyl-diaminobutyryl-diaminobutyryl-threonyl) Proteins 0.000 claims description 3
- 108010084794 deacylpolymyxin B Proteins 0.000 claims description 3
- 229940088598 enzyme Drugs 0.000 claims description 3
- 235000019253 formic acid Nutrition 0.000 claims description 3
- 230000009215 host defense mechanism Effects 0.000 claims description 3
- 108010093294 octapeptin antibiotics Proteins 0.000 claims description 3
- 108091005804 Peptidases Proteins 0.000 claims description 2
- 102000035195 Peptidases Human genes 0.000 claims description 2
- -1 deacylpolymyxin E Proteins 0.000 claims description 2
- 235000006408 oxalic acid Nutrition 0.000 claims description 2
- ODIGIKRIUKFKHP-UHFFFAOYSA-N (n-propan-2-yloxycarbonylanilino) acetate Chemical compound CC(C)OC(=O)N(OC(C)=O)C1=CC=CC=C1 ODIGIKRIUKFKHP-UHFFFAOYSA-N 0.000 claims 1
- OEDKDVKQFDPTHK-UBIDWWFKSA-N chembl526148 Chemical compound C([C@H]1C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(N)=O)C(=O)NCC(=O)N[C@H](C(=O)N2CCC[C@H]2C(=O)N[C@@H]2C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CO)C(=O)N[C@H]3CSSC[C@H]4C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@H](C(N1)=O)CSSC[C@H](NC(=O)[C@@H]1CCCN1C(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](CC=1C5=CC=CC=C5NC=1)NC(=O)[C@H](C(C)C)NC3=O)C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CSSC2)C(=O)N[C@@H](CO)C(=O)N4)=O)[C@@H](C)CC)C(C)C)[C@@H](C)CC)C1=CC=C(O)C=C1 OEDKDVKQFDPTHK-UBIDWWFKSA-N 0.000 claims 1
- 108010014869 circulin A Proteins 0.000 claims 1
- 239000003937 drug carrier Substances 0.000 claims 1
- 229940088710 antibiotic agent Drugs 0.000 description 19
- 241000588724 Escherichia coli Species 0.000 description 17
- ULGZDMOVFRHVEP-RWJQBGPGSA-N Erythromycin Chemical compound O([C@@H]1[C@@H](C)C(=O)O[C@@H]([C@@]([C@H](O)[C@@H](C)C(=O)[C@H](C)C[C@@](C)(O)[C@H](O[C@H]2[C@@H]([C@H](C[C@@H](C)O2)N(C)C)O)[C@H]1C)(C)O)CC)[C@H]1C[C@@](C)(OC)[C@@H](O)[C@H](C)O1 ULGZDMOVFRHVEP-RWJQBGPGSA-N 0.000 description 16
- 241000699670 Mus sp. Species 0.000 description 13
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 13
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 12
- 208000015181 infectious disease Diseases 0.000 description 11
- KDLRVYVGXIQJDK-AWPVFWJPSA-N clindamycin Chemical compound CN1C[C@H](CCC)C[C@H]1C(=O)N[C@H]([C@H](C)Cl)[C@@H]1[C@H](O)[C@H](O)[C@@H](O)[C@@H](SC)O1 KDLRVYVGXIQJDK-AWPVFWJPSA-N 0.000 description 9
- 229960003346 colistin Drugs 0.000 description 9
- 239000008367 deionised water Substances 0.000 description 9
- 229910021641 deionized water Inorganic materials 0.000 description 9
- KNIWPHSUTGNZST-UHFFFAOYSA-N polymyxin E2 Natural products CC(C)CCCCC(=O)NC(CCN)C(=O)NC(C(C)O)C(=O)NC(CCN)C(=O)NC1CCNC(=O)C(C(C)O)NC(=O)C(CCN)NC(=O)C(CCN)NC(=O)C(CC(C)C)NC(=O)C(CC(C)C)NC(=O)C(CCN)NC1=O KNIWPHSUTGNZST-UHFFFAOYSA-N 0.000 description 9
- 239000000243 solution Substances 0.000 description 9
- LRHPLDYGYMQRHN-UHFFFAOYSA-N N-Butanol Chemical compound CCCCO LRHPLDYGYMQRHN-UHFFFAOYSA-N 0.000 description 8
- 229960002227 clindamycin Drugs 0.000 description 8
- 229960003276 erythromycin Drugs 0.000 description 8
- 210000002966 serum Anatomy 0.000 description 7
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 239000012528 membrane Substances 0.000 description 6
- 230000001225 therapeutic effect Effects 0.000 description 6
- 241001625930 Luria Species 0.000 description 5
- 210000004027 cell Anatomy 0.000 description 5
- 239000002609 medium Substances 0.000 description 5
- 229940041153 polymyxins Drugs 0.000 description 5
- WNPBEUWOUYCJJR-UHFFFAOYSA-N 2-amino-n-[4-amino-1-oxo-1-[[6,9,18-tris(2-aminoethyl)-3-(1-hydroxyethyl)-12,15-bis(2-methylpropyl)-2,5,8,11,14,17,20-heptaoxo-1,4,7,10,13,16,19-heptazacyclotricos-21-yl]amino]butan-2-yl]-3-hydroxybutanamide Chemical compound CC(C)CC1NC(=O)C(CCN)NC(=O)C(NC(=O)C(CCN)NC(=O)C(N)C(C)O)CCNC(=O)C(C(C)O)NC(=O)C(CCN)NC(=O)C(CCN)NC(=O)C(CC(C)C)NC1=O WNPBEUWOUYCJJR-UHFFFAOYSA-N 0.000 description 4
- IECPWNUMDGFDKC-UHFFFAOYSA-N Fusicsaeure Natural products C12C(O)CC3C(=C(CCC=C(C)C)C(O)=O)C(OC(C)=O)CC3(C)C1(C)CCC1C2(C)CCC(O)C1C IECPWNUMDGFDKC-UHFFFAOYSA-N 0.000 description 4
- SBKRTALNRRAOJP-BWSIXKJUSA-N N-[(2S)-4-amino-1-[[(2S,3R)-1-[[(2S)-4-amino-1-oxo-1-[[(3S,6S,9S,12S,15R,18R,21S)-6,9,18-tris(2-aminoethyl)-15-benzyl-3-[(1R)-1-hydroxyethyl]-12-(2-methylpropyl)-2,5,8,11,14,17,20-heptaoxo-1,4,7,10,13,16,19-heptazacyclotricos-21-yl]amino]butan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-1-oxobutan-2-yl]-6-methylheptanamide (6S)-N-[(2S)-4-amino-1-[[(2S,3R)-1-[[(2S)-4-amino-1-oxo-1-[[(3S,6S,9S,12S,15R,18R,21S)-6,9,18-tris(2-aminoethyl)-15-benzyl-3-[(1R)-1-hydroxyethyl]-12-(2-methylpropyl)-2,5,8,11,14,17,20-heptaoxo-1,4,7,10,13,16,19-heptazacyclotricos-21-yl]amino]butan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-1-oxobutan-2-yl]-6-methyloctanamide sulfuric acid Polymers OS(O)(=O)=O.CC(C)CCCCC(=O)N[C@@H](CCN)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCN)C(=O)N[C@H]1CCNC(=O)[C@@H](NC(=O)[C@H](CCN)NC(=O)[C@H](CCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](Cc2ccccc2)NC(=O)[C@@H](CCN)NC1=O)[C@@H](C)O.CC[C@H](C)CCCCC(=O)N[C@@H](CCN)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCN)C(=O)N[C@H]1CCNC(=O)[C@@H](NC(=O)[C@H](CCN)NC(=O)[C@H](CCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](Cc2ccccc2)NC(=O)[C@@H](CCN)NC1=O)[C@@H](C)O SBKRTALNRRAOJP-BWSIXKJUSA-N 0.000 description 4
- JUJWROOIHBZHMG-UHFFFAOYSA-N Pyridine Chemical compound C1=CC=NC=C1 JUJWROOIHBZHMG-UHFFFAOYSA-N 0.000 description 4
- 241000293869 Salmonella enterica subsp. enterica serovar Typhimurium Species 0.000 description 4
- 108010058601 colistin nonapeptide Proteins 0.000 description 4
- 229960004675 fusidic acid Drugs 0.000 description 4
- IECPWNUMDGFDKC-MZJAQBGESA-N fusidic acid Chemical compound O[C@@H]([C@@H]12)C[C@H]3\C(=C(/CCC=C(C)C)C(O)=O)[C@@H](OC(C)=O)C[C@]3(C)[C@@]2(C)CC[C@@H]2[C@]1(C)CC[C@@H](O)[C@H]2C IECPWNUMDGFDKC-MZJAQBGESA-N 0.000 description 4
- 238000002347 injection Methods 0.000 description 4
- 239000007924 injection Substances 0.000 description 4
- FEMOMIGRRWSMCU-UHFFFAOYSA-N ninhydrin Chemical compound C1=CC=C2C(=O)C(O)(O)C(=O)C2=C1 FEMOMIGRRWSMCU-UHFFFAOYSA-N 0.000 description 4
- 239000002953 phosphate buffered saline Substances 0.000 description 4
- 229960003548 polymyxin b sulfate Drugs 0.000 description 4
- 238000002360 preparation method Methods 0.000 description 4
- 230000002829 reductive effect Effects 0.000 description 4
- 159000000000 sodium salts Chemical class 0.000 description 4
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 3
- 241000607142 Salmonella Species 0.000 description 3
- YXFVVABEGXRONW-UHFFFAOYSA-N Toluene Chemical compound CC1=CC=CC=C1 YXFVVABEGXRONW-UHFFFAOYSA-N 0.000 description 3
- 230000003698 anagen phase Effects 0.000 description 3
- 230000001580 bacterial effect Effects 0.000 description 3
- 230000004888 barrier function Effects 0.000 description 3
- 230000003115 biocidal effect Effects 0.000 description 3
- 230000002255 enzymatic effect Effects 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 125000005313 fatty acid group Chemical group 0.000 description 3
- 230000002401 inhibitory effect Effects 0.000 description 3
- 239000002244 precipitate Substances 0.000 description 3
- 239000002904 solvent Substances 0.000 description 3
- 239000000725 suspension Substances 0.000 description 3
- 238000004809 thin layer chromatography Methods 0.000 description 3
- 229920001817 Agar Polymers 0.000 description 2
- 108090000604 Hydrolases Proteins 0.000 description 2
- 102000004157 Hydrolases Human genes 0.000 description 2
- YJQPYGGHQPGBLI-UHFFFAOYSA-N Novobiocin Natural products O1C(C)(C)C(OC)C(OC(N)=O)C(O)C1OC1=CC=C(C(O)=C(NC(=O)C=2C=C(CC=C(C)C)C(O)=CC=2)C(=O)O2)C2=C1C YJQPYGGHQPGBLI-UHFFFAOYSA-N 0.000 description 2
- 241000405383 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 Species 0.000 description 2
- 229920005654 Sephadex Polymers 0.000 description 2
- 239000012507 Sephadex™ Substances 0.000 description 2
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 2
- 229920000392 Zymosan Polymers 0.000 description 2
- MHLMRBVCMNDOCW-UHFFFAOYSA-N acetic acid;butan-1-ol;hydrate Chemical compound O.CC(O)=O.CCCCO MHLMRBVCMNDOCW-UHFFFAOYSA-N 0.000 description 2
- 239000008272 agar Substances 0.000 description 2
- 125000003277 amino group Chemical group 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 238000009835 boiling Methods 0.000 description 2
- 239000001913 cellulose Substances 0.000 description 2
- 229920002678 cellulose Polymers 0.000 description 2
- 229960003326 cloxacillin Drugs 0.000 description 2
- LQOLIRLGBULYKD-JKIFEVAISA-N cloxacillin Chemical compound N([C@@H]1C(N2[C@H](C(C)(C)S[C@@H]21)C(O)=O)=O)C(=O)C1=C(C)ON=C1C1=CC=CC=C1Cl LQOLIRLGBULYKD-JKIFEVAISA-N 0.000 description 2
- 230000008260 defense mechanism Effects 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 230000012010 growth Effects 0.000 description 2
- 230000002147 killing effect Effects 0.000 description 2
- 229960000515 nafcillin Drugs 0.000 description 2
- GPXLMGHLHQJAGZ-JTDSTZFVSA-N nafcillin Chemical compound C1=CC=CC2=C(C(=O)N[C@@H]3C(N4[C@H](C(C)(C)S[C@@H]43)C(O)=O)=O)C(OCC)=CC=C21 GPXLMGHLHQJAGZ-JTDSTZFVSA-N 0.000 description 2
- 229960002950 novobiocin Drugs 0.000 description 2
- YJQPYGGHQPGBLI-KGSXXDOSSA-N novobiocin Chemical compound O1C(C)(C)[C@H](OC)[C@@H](OC(N)=O)[C@@H](O)[C@@H]1OC1=CC=C(C(O)=C(NC(=O)C=2C=C(CC=C(C)C)C(O)=CC=2)C(=O)O2)C2=C1C YJQPYGGHQPGBLI-KGSXXDOSSA-N 0.000 description 2
- 238000013421 nuclear magnetic resonance imaging Methods 0.000 description 2
- 230000003287 optical effect Effects 0.000 description 2
- 230000035515 penetration Effects 0.000 description 2
- UMJSCPRVCHMLSP-UHFFFAOYSA-N pyridine Natural products COC1=CC=CN=C1 UMJSCPRVCHMLSP-UHFFFAOYSA-N 0.000 description 2
- 239000011347 resin Substances 0.000 description 2
- 229920005989 resin Polymers 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- WFIYPADYPQQLNN-UHFFFAOYSA-N 2-[2-(4-bromopyrazol-1-yl)ethyl]isoindole-1,3-dione Chemical compound C1=C(Br)C=NN1CCN1C(=O)C2=CC=CC=C2C1=O WFIYPADYPQQLNN-UHFFFAOYSA-N 0.000 description 1
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 1
- 229930186147 Cephalosporin Natural products 0.000 description 1
- 108010073254 Colicins Proteins 0.000 description 1
- 241000206602 Eukaryota Species 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- OJMMVQQUTAEWLP-UHFFFAOYSA-N Lincomycin Natural products CN1CC(CCC)CC1C(=O)NC(C(C)O)C1C(O)C(O)C(O)C(SC)O1 OJMMVQQUTAEWLP-UHFFFAOYSA-N 0.000 description 1
- 201000009906 Meningitis Diseases 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 229930182555 Penicillin Natural products 0.000 description 1
- 206010057249 Phagocytosis Diseases 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 206010040047 Sepsis Diseases 0.000 description 1
- 108010056079 Subtilisins Proteins 0.000 description 1
- 102000005158 Subtilisins Human genes 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 239000002390 adhesive tape Substances 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
- 229940024606 amino acid Drugs 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
- 239000004599 antimicrobial Substances 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- SAKUKAQFBMDKGX-UHFFFAOYSA-N butan-1-ol;2-pyridin-2-ylacetic acid;hydrate Chemical compound O.CCCCO.OC(=O)CC1=CC=CC=N1 SAKUKAQFBMDKGX-UHFFFAOYSA-N 0.000 description 1
- 229960003669 carbenicillin Drugs 0.000 description 1
- FPPNZSSZRUTDAP-UWFZAAFLSA-N carbenicillin Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)C(C(O)=O)C1=CC=CC=C1 FPPNZSSZRUTDAP-UWFZAAFLSA-N 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 229940124587 cephalosporin Drugs 0.000 description 1
- 150000001780 cephalosporins Chemical class 0.000 description 1
- 210000001175 cerebrospinal fluid Anatomy 0.000 description 1
- 229920001429 chelating resin Polymers 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 229960001200 clindamycin hydrochloride Drugs 0.000 description 1
- 230000020176 deacylation Effects 0.000 description 1
- 238000005947 deacylation reaction Methods 0.000 description 1
- 230000007123 defense Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 239000003480 eluent Substances 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 230000007071 enzymatic hydrolysis Effects 0.000 description 1
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 description 1
- 229960000741 erythromycin ethylsuccinate Drugs 0.000 description 1
- NSYZCCDSJNWWJL-YXOIYICCSA-N erythromycin ethylsuccinate Chemical compound O1[C@H](C)C[C@H](N(C)C)[C@@H](OC(=O)CCC(=O)OCC)[C@@H]1O[C@H]1[C@@](O)(C)C[C@@H](C)C(=O)[C@H](C)[C@@H](O)[C@](C)(O)[C@@H](CC)OC(=O)[C@H](C)[C@@H](O[C@@H]2O[C@@H](C)[C@H](O)[C@](C)(OC)C2)[C@@H]1C NSYZCCDSJNWWJL-YXOIYICCSA-N 0.000 description 1
- 125000004494 ethyl ester group Chemical group 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 239000012847 fine chemical Substances 0.000 description 1
- 239000011888 foil Substances 0.000 description 1
- 230000006870 function Effects 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 231100001231 less toxic Toxicity 0.000 description 1
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- OJMMVQQUTAEWLP-KIDUDLJLSA-N lincomycin Chemical compound CN1C[C@H](CCC)C[C@H]1C(=O)N[C@H]([C@@H](C)O)[C@@H]1[C@H](O)[C@H](O)[C@@H](O)[C@@H](SC)O1 OJMMVQQUTAEWLP-KIDUDLJLSA-N 0.000 description 1
- 229960005287 lincomycin Drugs 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 238000004816 paper chromatography Methods 0.000 description 1
- 229940049954 penicillin Drugs 0.000 description 1
- 235000019371 penicillin G benzathine Nutrition 0.000 description 1
- 229940056360 penicillin g Drugs 0.000 description 1
- 230000035699 permeability Effects 0.000 description 1
- 230000008782 phagocytosis Effects 0.000 description 1
- 239000008194 pharmaceutical composition Substances 0.000 description 1
- 239000008057 potassium phosphate buffer Substances 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 230000001681 protective effect Effects 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 230000005180 public health Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 239000011550 stock solution Substances 0.000 description 1
- 229910021653 sulphate ion Inorganic materials 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
- C07K7/50—Cyclic peptides containing at least one abnormal peptide link
- C07K7/54—Cyclic peptides containing at least one abnormal peptide link with at least one abnormal peptide link in the ring
- C07K7/60—Cyclic peptides containing at least one abnormal peptide link with at least one abnormal peptide link in the ring the cyclisation occurring through the 4-amino group of 2,4-diamino-butanoic acid
- C07K7/62—Polymyxins; Related peptides
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S930/00—Peptide or protein sequence
- Y10S930/01—Peptide or protein sequence
- Y10S930/19—Antibiotic
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S930/00—Peptide or protein sequence
- Y10S930/01—Peptide or protein sequence
- Y10S930/27—Cyclic peptide or cyclic protein
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Animal Behavior & Ethology (AREA)
- Oncology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Communicable Diseases (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Pharmacology & Pharmacy (AREA)
- General Chemical & Material Sciences (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB08228545A GB2128617A (en) | 1982-10-06 | 1982-10-06 | Polypeptides for use in antibacterial therapy |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| NO833633L true NO833633L (no) | 1984-04-09 |
Family
ID=10533423
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO833633A NO833633L (no) | 1982-10-06 | 1983-10-05 | Nye forbindelser for bruk i antibakteriell terapi |
Country Status (9)
| Country | Link |
|---|---|
| US (1) | US4510132A (fi) |
| EP (1) | EP0113394A1 (fi) |
| JP (1) | JPS59134764A (fi) |
| AU (1) | AU1911983A (fi) |
| DK (1) | DK450083A (fi) |
| FI (1) | FI833612A (fi) |
| GB (1) | GB2128617A (fi) |
| NO (1) | NO833633L (fi) |
| ZA (1) | ZA836977B (fi) |
Families Citing this family (25)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CA1267374A (en) * | 1984-09-07 | 1990-04-03 | George Boguslawski | Enhanced inhibition of yeast cell growth |
| EP0333243A3 (en) * | 1988-03-10 | 1989-09-27 | Akzo N.V. | Sulphated k5 antigen and sulphated k5 antigen fragments |
| NL9101390A (nl) * | 1991-08-15 | 1993-03-01 | Barend Willem Hak | Werkwijze ter bereiding van een antiseptisch preparaat. |
| US5658560A (en) * | 1994-01-18 | 1997-08-19 | Serikov; Vladimir B. | Method of treating endotoxemia by administering tyloxapol |
| US6180604B1 (en) * | 1996-08-21 | 2001-01-30 | Micrologix Biotech Inc. | Compositions and methods for treating infections using analogues of indolicidin |
| US6503881B2 (en) | 1996-08-21 | 2003-01-07 | Micrologix Biotech Inc. | Compositions and methods for treating infections using cationic peptides alone or in combination with antibiotics |
| CA2301336A1 (en) * | 2000-03-17 | 2001-09-17 | Michael T. Kelly | Topical treatment of rosacea |
| US6835536B2 (en) | 2001-08-21 | 2004-12-28 | Micrologix Biotech Inc. | Antimicrobial cationic peptides and formulations thereof |
| US20060004185A1 (en) * | 2004-07-01 | 2006-01-05 | Leese Richard A | Peptide antibiotics and peptide intermediates for their prepartion |
| US7802738B2 (en) * | 2004-07-16 | 2010-09-28 | Nelson Irrigation Corporation | Power-assisted docking station for mobile irrigation apparatus |
| US7807637B2 (en) * | 2006-08-11 | 2010-10-05 | Northern Antibiotics Oy | Polymyxin derivatives and uses thereof |
| CN103059106B (zh) | 2006-08-11 | 2015-01-14 | 北方抗生素有限公司 | 多粘菌素衍生物及其用途 |
| US8193148B2 (en) | 2008-02-08 | 2012-06-05 | Northern Antibiotics Ltd. | Short fatty acid tail polymyxin derivatives and uses thereof |
| US9096649B2 (en) | 2008-02-08 | 2015-08-04 | Northern Antibiotics Ltd. | Polymyxin derivatives and uses thereof |
| US8329645B2 (en) * | 2008-02-08 | 2012-12-11 | Northern Antibiotics Ltd. | Polymyxin derivatives and uses thereof |
| FI20085469A0 (fi) | 2008-02-08 | 2008-05-16 | Northern Antibiotics Oy | Polymyksiinijohdannaiset, joissa on lyhyt rasvahappohäntä, ja niiden käyttöjä |
| US8343912B2 (en) | 2008-12-23 | 2013-01-01 | Biosource Pharm, Inc. | Antibiotic compositions for the treatment of gram negative infections |
| US8415307B1 (en) | 2010-06-23 | 2013-04-09 | Biosource Pharm, Inc. | Antibiotic compositions for the treatment of gram negative infections |
| BR112014012016A2 (pt) | 2011-11-18 | 2017-05-16 | Cantab Anti-Infectives Ltd | compostos |
| SI2999711T1 (sl) | 2013-05-22 | 2022-10-28 | Spero Therapeutics, Inc. | Derivati polimiksina in njihova uporaba v kombinacijskem zdravljenju skupaj z različnimi antibiotiki |
| FR3057463B1 (fr) * | 2016-10-13 | 2019-07-12 | Fondation Mediterranee Infection | Association de composes antibiotiques efficace contre des enterobacteries |
| US11191773B2 (en) * | 2017-07-17 | 2021-12-07 | President And Fellows Of Harvard College | Methods of treatment for bacterial infections |
| WO2019084628A1 (en) * | 2017-11-02 | 2019-05-09 | The University Of Queensland | Peptide antibiotics |
| WO2019178119A1 (en) | 2018-03-12 | 2019-09-19 | President And Fellows Of Harvard College | Aminocoumarin compounds and methods of their use |
| EP4316504A3 (en) | 2018-06-25 | 2024-04-17 | Spero Therapeutics, Inc. | Compounds |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US2695261A (en) * | 1946-12-21 | 1954-11-23 | Burroughs Wellcome Co | Production of polymyxins a, b, and e |
| US2759868A (en) * | 1948-08-05 | 1956-08-21 | Burroughs Wellcome Co | Manufacture of polymyxins b and e |
| BE754411A (fr) * | 1969-08-05 | 1971-02-04 | Rhone Poulenc Sa | Cyclopeptides derives des polymyxines et leur |
| FR2124060B1 (fi) * | 1971-02-02 | 1974-04-12 | Rhone Poulenc Sa | |
| US4252795A (en) * | 1978-09-11 | 1981-02-24 | Ayerst Mckenna And Harrison Inc. | N-substituted dimeric cyclopeptide derivatives and preparation thereof |
| US4237045A (en) * | 1978-09-11 | 1980-12-02 | American Home Products Corporation | N-substituted cyclopeptide derivatives and preparation thereof |
-
1982
- 1982-10-06 GB GB08228545A patent/GB2128617A/en not_active Withdrawn
-
1983
- 1983-09-14 AU AU19119/83A patent/AU1911983A/en not_active Abandoned
- 1983-09-20 ZA ZA836977A patent/ZA836977B/xx unknown
- 1983-09-22 US US06/534,617 patent/US4510132A/en not_active Expired - Fee Related
- 1983-09-29 DK DK450083A patent/DK450083A/da not_active Application Discontinuation
- 1983-10-05 FI FI833612A patent/FI833612A/fi not_active Application Discontinuation
- 1983-10-05 EP EP83109962A patent/EP0113394A1/en not_active Withdrawn
- 1983-10-05 NO NO833633A patent/NO833633L/no unknown
- 1983-10-06 JP JP58186076A patent/JPS59134764A/ja active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| EP0113394A1 (en) | 1984-07-18 |
| JPS59134764A (ja) | 1984-08-02 |
| DK450083A (da) | 1984-04-07 |
| US4510132A (en) | 1985-04-09 |
| GB2128617A (en) | 1984-05-02 |
| ZA836977B (en) | 1984-05-30 |
| FI833612A (fi) | 1984-04-07 |
| FI833612A0 (fi) | 1983-10-05 |
| DK450083D0 (da) | 1983-09-29 |
| AU1911983A (en) | 1984-04-12 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| NO833633L (no) | Nye forbindelser for bruk i antibakteriell terapi | |
| Vanittanakom et al. | Fengycin-a novel antifungal lipopeptide antibiotic produced by Bacillus subtilis F-29-3 | |
| Somma et al. | Teicoplanin, a new antibiotic from Actinoplanes teichomyceticus nov. sp | |
| Gerasimenko et al. | Antibacterial effects of water-soluble low-molecular-weight chitosans on different microorganisms | |
| Hammond et al. | A new class of synthetic antibacterials acting on lipopolysaccharide biosynthesis | |
| Somner et al. | Inhibition of peptidoglycan biosynthesis by ramoplanin | |
| Vaara et al. | Sensitization of Gram-negative bacteria to antibiotics and complement by a nontoxic oligopeptide | |
| Vaara et al. | Group of peptides that act synergistically with hydrophobic antibiotics against gram-negative enteric bacteria | |
| Fett et al. | Characterization of exopolysaccharides produced by plant-associated fluorescent pseudomonads | |
| US5576298A (en) | Peptides from pseudomonas syringae possessing broad-spectrum antibiotic activity | |
| Woodruff et al. | Microbiological aspects of penicillin: VII. Bacterial penicillinase | |
| EP0182315A2 (en) | Novel antibiotic NK84-0218 pharmaceutical compositions containing it and process for the production of the same | |
| Park et al. | Staphylococcus aureus and Micrococcus luteus peptidoglycan transglycosylases that are not penicillin-binding proteins | |
| CA2243067A1 (en) | Adhesion inhibitors, preparation comprising them and method for producing them | |
| Slomiany et al. | Glycosulfatase activity of Helicobacter pylori toward gastric mucin | |
| Williams | Sub-MICs of cefuroxime and ciprofloxacin influence interaction of complement and immunoglobulins with Klebsiella pneumoniae | |
| US5648455A (en) | Antibiotic WAP-8294A, method for preparing the same and antibacterial composition | |
| Ozer et al. | Derepression of β-Lactamase (Penicillinase) in Bacillus cereus by Peptidoglycans | |
| CA1228824A (en) | Antibiotic and process for the production thereof | |
| CA1100876A (en) | Use of a nitrogen-containing polysaccharide for promoting drug-sensitivity of bacteria resistant to antibiotics | |
| JP3811326B2 (ja) | 抗真菌剤とその利用 | |
| Knüsel et al. | Sideromycins | |
| US3089827A (en) | Process for preparing zygomycins | |
| US4513083A (en) | Preparation of an antibiotic selectively effective against staphylococcus infections | |
| Lin et al. | Isolation, purification, and physical and chemical properties of neuraminidase inhibitor No. 289 |