KR19980702853A - Amphiphilic Peptides and Analogs thereof - Google Patents

Abstract

The present invention relates to amphipathic peptides and analogs thereof. The specification defines molecules in three ways and discloses improved antimicrobial peptides having improved antimicrobial properties, consisting of sequences selected from the following groups:

+-++-++-+-++, +-++-++ --- +-++, ++-+++-++-+++-, + +-+++-++-++++-++-, ++-+++-++-++-++-,-++-++-++- -++-++, ++++-+++-+-++, ++-+++++++-++-++-, where + represents a hydrophobic amino acid residue And-represents a hydrophilic amino acid residue. The specific sequence of the active peptide is shown. The specification also discloses two general formulas defining rules, whereby identifying peptides falling within the scope of the present invention.

Description

Amphiphilic Peptides and Analogs thereof

Peptides are polymers of amino acids. There are about 20 natural amino acids, which differ somewhat in their chemistry. By arranging specific amino acid sequences within peptide molecules, it is possible to obtain peptides that exhibit a very wide range of chemical functionality, ranging from activity as a catalyst (eg enzymes) to chemical messengers (eg peptide hormones such as insulin). . Small changes in peptide sequences are known to have significant consequences on the functionality of molecules. It is known that the synthesis of particular peptides can be directed by nucleic acid molecules having related sequences.

Amphiphilic peptides are characterized by amino acid structures that provide some regions of hydrophobic properties and other regions of hydrophilic properties. It is believed that such peptides can interact with the membranes of living cells to modify the life processes of the cells. Many amphipathic peptides exist naturally, and other amphiphilic peptides have been produced by synthetic methods.

International application 92/01462 discloses amphipathic peptides for inhibiting growth of target cells. This peptide is composed of both hydrophobic and hydrophilic amino acid residues. The balance of hydrophobicity and hydrophilicity of amino acids can be described by the literature on hydrophobicity values cited by Eisenberg et al. (Nature 1982 299, p. 371). Hydrophobic residues have a value greater than zero while hydrophilic residues have a value less than zero.

For convenience, some of these values are shown in Table 1 below along with the codes used to indicate associated amino acid residues.

value Residue 0.530.250.610.540.730.16-0.18-0.26-0.62-0.69-1.1-1.76 L = leucine A = alanine F = phenylalanine V = valine I = isoleucine G = glycine T = threonine S = serine E = glutamate Q = glutamine K = lysine R = arginine

In International Application No. 92/01462, hydrophobic residues are denoted by + and hydrophilic residues are denoted by-++-++-++-+-,-++-+ -++-++, +-++-++-+-++-+ and +-++-++-+-++-+ Peptides are disclosed. Specific peptides disclosed include peptides having a sequence of LKLLKKLLKKLKKLLKKL. Lee et al. Disclose an amphiphilic antimicrobial peptide having the following structure in Biochimica et Biophysica Acta 862 (1986) pages 211-219: Ac- (LARL) _1-4 -NHCH ₃ , Ac- ( LLARL) _2-3 -NHCH ₃ , Ac- (ARL) _3-4 -NHCH ₃ and Ac- (LAKL) _2-3 -NHCH ₃ . Introductory commentary in this area is provided in Biochimica et Biophysica Acta 1197 (1994), pages 109-131.

Despite the sequence of several amphiphilic peptides known, it has proven difficult to identify these peptides, particularly with high antimicrobial activity. In theory, it would take quite a long time while each possible peptide would be difficult to synthesize and test for bacteria, fungi and other microorganisms, and to evaluate the numerous possible amino acid sequences of a given appropriate length. Thus, there is a need to identify and identify those peptides that are expected to be effective by other than just identification based on in-vitro functional testing of molecules that are expensive to synthesize.

Brief description of the invention

We have found that improved amphipathic antimicrobial peptides can be prepared consisting of sequences selected from the following groups:

+-++-++-+-++,

+-++-++ --- +-++,

++-+++-++-+++-,

++-+++-++-++++-++-,

++-+++-++-++-++-,

-++-++-++-++-++,

++++-+++-+-++,

++-+++++++-++-++-,

++-++-++-++-++-++,

++-++-++-++-++,

++-+-++-++-++,

-++ --- ++-++-++-++, and

++-++-+-++-++-++.

Of these, + represents hydrophobic amino acid residues, and-represents hydrophilic amino acid residues.

In particular, we found utility in peptides having the following sequence:

(MB_00) SEQ ID NO: 1 LKLLKKLLKKLKKLL,

(MB_18) SEQ ID NO: 2 LKALKKLAKKKLKKLA,

(MB_21) SEQ ID NO: 3 FASLLGKALKALAKQ,

(MB_36) SEQ ID NO: 4 FASLLGKALKALLAKLAKQ,

(MB_37) SEQ ID NO: 5 FASLLGKLAKKLAKKALK,

(MB_47) SEQ ID NO: 6 QKAASRLLRALSKLLEAF,

(CM_1) SEQ ID NO: 7 LALLKVLLRKIKKAL,

(CM_3) SEQ ID NO: 8 ALKAALLAILKIVRVIKK,

(MC_03) SEQ ID NO: 9 AASKAAKTLAKLLSSLLKLL,

(MC_04) SEQ ID NO: 10 LLKKLLRAASKALSLL,

(MC_05) SEQ ID NO: 11 AAKKLSKLLKTLLKLL,

(MC_08) SEQ ID NO: 12 KALKKKLLKLASSKKTAL,

(MC_10) SEQ ID NO: 13 AASKALRTASRLARSLLTLL.

Among the above sequences, L = leucine, A = alanine, F = phenylalanine, V = valine, I = isoleucine, G = glycine, K = lysine, S = serine, E = glutamate, Q = glutamine, T = threonine and R Arginine.

We also found that effective antimicrobial and ineffective peptides were identified through vector analysis of the dimensions corresponding to charge, hydrophilic / lipophilic balance, hydrophobic moment, and amphiphilicity of the peptides, whereby It is determined that the film is placed in the counterclockwise direction of the amphipathic dimension and the clockwise direction of the charge dimension.

Furthermore, we determined that by identifying the peptides that correlate specific physical properties with their biological activity against a particular microorganism, effective and ineffective peptides are identified.

As discussed above, it will be appreciated that a very large number of possible peptides can have a chain length of 10-30 amino acids. We have determined what the general rule for peptides with effective antimicrobial properties is, and as discussed in more detail below, there is a strong correlation between peptides that meet this law and peptides with effective antimicrobial properties. Said. Conversely, many of the peptides exhibiting properties outside the scope of this law do not appear to exhibit effective antimicrobial properties.

Thus, the present invention provides that the predicted log sterilization value (L _{S aureus} ) for _{S. aureus} ATCC 6538 is greater than 5, and L _{S aureus} is equal to the equation L _{S aureus} = y [25] * (4.8362068) + (3.5316215). Extended to antimicrobial peptides having a length of 10-30 amino acid residues.

In the above formula,

In the above formula,

z ₁ = sum of hydrophobic and hydrophilic values

z ₂ = Y component of the charge dipole

z ₃ = sum of negative charges

z ₄ = Approximate value for sine curve

z ₅ = X component of the charge dipole

z ₆ = Approximate fit to square curve

The present invention provides a logarithmic sterilization value (L _{E coli} ) for E. coli ATCC 11229 that is greater than 4, and that L _{E coli} is given by the equation L _{E coli} = y [27] * (4.41875) + (3.615). Extends to antimicrobial peptides having a length of 30 amino acid residues.

In the above formula,

z ₀ is L _{S aureus} ,

z ₁ is the molecular weight,

z ₂ is the modulus of the hydrophobic dipole moment in the Z-plane,

z ₃ is a hydrophobic solvent accessible surface,

z ₄ is the number of atoms greater than 8 μs from the alpha helix axis,

z ₅ is the 2D diameter (R _xy ) of the gyration

Although the equations mentioned above seem complicated, this is a simple computer task to determine whether any particular peptide is within the scope of the law. Equations are the so-called equations of neural networks, and the general type is well known to those skilled in the art.

As discussed in detail below and demonstrated by the examples, it is possible to find sequences that are expected to follow this law with a given law and eventually exhibit significant antimicrobial properties. Thus, the synthesis of peptides identified as potentially antimicrobial is a considerably simpler task than the synthesis of peptides based on the measured antimicrobial and selection of preferred molecules.

The present invention relates to amphiphilic peptides and analogs thereof.

In the present specification, the following terms are used.

Molecular weight is the molecular weight of the peptide expressed in daltons (g / mol).

Hydrophobic solvent accessible surfaces (square of K) are determined using the SYBYL [TM] molecular model package (eg TRISPOS [TM]). Hydrophilic solvent accessible surface (square of power) is determined using SYBYL [TM] molecular modeling package (eg TRISPOS [TM]).

The X- and Y-components of the charge dipole are from SYBYL after aligning the molecules such that the z-axis is along the long axis of the molecule, i.e., the axis of the helix, and the y axis is projected and aligned into a plane perpendicular to the z-axis of the vector p. Can be obtained.

In the above, P = H _i C _i is the sum of the hydrophobic residues, where

C _i = center of gravity of the alpha-carbon of each residue,

H _i = hydrophobicity of the residue according to Eisenberg.

The sum of negative charges is the sum of the negative charges on the residues at pH 7.0.

Hydrophobic dipole moment is a vector in the XY- plane H ⁺ -H ^- the sum of. From here,

H ⁺ = sum of hydrophobic residues of H _i C _i ^XY ,

H ^- is the sum of the hydrophilic moiety of the _i = H C _i ^XY.

The sum of the hydrophobic and hydrophilic values is the sum of the hydrophobic and hydrophilic values according to Eisenberg (cit. Ultra).

Coefficient of hydrophobic dipole moment in the Z-plane. This hydrophobic dipole moment H _z is given by the following equation.

^{_{H z = H z + - H}} z -

In the above formula, H _z ⁺ is the sum of (H _i * Z _i ) among all hydrophobic amino acids, H _z ⁻ is the sum of (-H _i * Z _i ) among all hydrophilic amino acids, and H _i is the eigen of amino acid i Is bug (c. Ultra) hydrophobic, Z _i is the z-coordinate of the C-alpha carbon atom of amino acid i, expressed in units of 되며 and the coordinates are described above, i.e. the Z-axis is the long axis side of the molecule. Use a coordinate system in which the molecules are aligned as much as possible.

Numerous atoms from SYBYL can be obtained from SYBYL that are at least 8 ms from the axis of the alpha helix.

The approximation S _{sin, which} is suitable for a sine curve, is given by the following least squares equation:

S _sin = Min _θ {Σ _i ^N [H _i -sin (100i-θ)] ² } / N

Wherein N is the number of peptides and S _sin is the minimum value that can be obtained by changing the starting value θ, where H _i is the largest positive value and the largest negative value of the hydrophobicity for the residue, respectively This is the value when normalized to be set to 1 and -1.

An approximation S _sqr that fits the square curve is given by the following least squares equation:

S _sqr = Min _θ {Σ _i ^N {0.5 * [sign (H _i )-sign (sin (100i-θ))] ² }}

Wherein N is the number of amino acid residues and H _i is a hydrophobic value, for example S _sqr is the minimum value that can be obtained by changing the starting value θ.

The gyration diameter (R _xyz ) is a known measure of the sphericalness of the molecule. The 2D diameter of the pivot (R _xy ) relates to how circular the peptide looks when looking down the alpha helix axis.

R _xy ² = Σ _i ^N [X _i ² + Y _i ² ]) / N)

In the formula, X_i And Y_iIs the coordinate of atom I. N is the number of atoms in the peptide. This value is believed to be related to the ease of diffusion of molecules through the outer membrane of E. coli.

The software used was version SYBYL 6.2 (R400 running on Silicon Graphics [TM] Powder Challenge [TM]). Peptides were assembled using a biopolymer module, and individual peptides in alpha helix shape were assembled using the command BIOPOLYMER BUILD M1SEQUENCE ALPHA_HELIX. Subsequently, hydrogen atoms were added using the command BIOPOLYMER ADDH M1 ( ^* ) ESSENTIAL_ONLY. The peptide was then oriented as specified above, and then the protein structure was refined using the following command.

BIOPOLYMER ADD_SIDECHAINS M1 ( ^* )

BIOPOLYMER FIX_AND_GROUPS M1 NEUTRAL

BIOPOLYMER ADDH M1 ( ^* ) ALL

The charge was calculated using the Gastiger-Huckel method. All of the calculations mentioned above can be automated using computer technology.

The forcefield used is M. M. Clark, R. D. Cramer, III and N. N. van Opdenbosch [J. Comp. Chem, Vol 10, p982-1012 (1989), and Triforce 5.2 Forcefield modified for the release of SYBYL 6.0 as described in Appendix 2 of the Sybyl Theory Guide.

From the above, it can be seen that the variables used to define the peptides according to the invention can simply be determined in a given peptide structure and it is not necessary to measure the actual physical parameters of the peptides at all. This process can be performed by a computer. Given that there are a limited number of peptide molecules with 10-30 amino acids, the sequence and parameters of each of these peptides are determined and then the predicted log sterilization value for E. coli or S. aureus above that required for the peptide. Determining whether or not there is a simple task by the computer.

The aforementioned peptides have some additional features that are particularly suitable as amphiphilic antimicrobial peptides.

While helixes of D-amino acids are believed to be effective, peptides are generally L-configuration.

The peptides according to the invention are predominantly alpha-helical and amphiphilic in their secondary structure in that one side has two distinct aspects that are predominantly hydrophilic and the other is hydrophobic.

The peptide is relatively short with 12-26, preferably 13-20, most preferably 15-18 amino acid residues. These relatively short chain lengths are believed to reduce the risk of hematopoietic toxicity.

Preferably, the peptide is rich in basic amino acids, in particular lysine and arginine. In a preferred embodiment, 15-50% of the number of amino acid residues present is lysine or arginine.

Preferably, the peptide lacks so-called beta-rotating formers, in particular iso-leucine, tyrosine and valine. In a preferred embodiment of the invention, less than 20% of the number of amino acid residues present are iso-leucine, tyrosine or valine.

The numerical ratio of the number of lysine or arginine residues to the number of iso-leucine, tyrosine or valine residues is preferably at least one.

Preferably, the peptide is rich in alpha-helix formers, in particular lysine, alanine and glutamine. It is preferred that at least 50% of the number of amino acid residues is lysine, alanine or glutamine.

Preferably, the net amount of charge in total is positive so that the molecule is a cation at pH 7.00.

Preferably, special amino acids such as cysteine, proline and histidine are not predominant. In an aspect of the invention, these amino acids are typically absent.

Preferably, the peptide has an amphipathy of 0.15 to -0.34. Amphiphilicity for a peptide with N residues is obtained by subtracting the sum of H _n (hydrophilic side) from 1-N from the sum of H _n (hydrophobic side) from 1-N: where H _n is Eisenberg Is the hydrophobicity of the nth residue as given by.

Preferably, the peptide has a hydrophobic moment of 0.25 to 0.5. The hydrophobic moment is the scalar amount derived from the vector sum of the hydrophobic moments of the individual residues divided by the total number of residues. The hydrophobic moment for the peptide having N residues is obtained by the following formula.

(1 / N) {[Σ ^N _{i = 1} H _i .sin (δ _i )] ² + [Σ ^N _{i = 1} H _i .cos (δ _i )] ² } ^1/2

Wherein N is the number of residues, H _i is the hydrophobicity of the i th residue and δ _i is the angle between the unit vectors of consecutive residues, ie 100 degrees.

Preferably, the peptide has both L _s 5 and L _e 5 in length of amino acids 13-20 and consists of at least three residues of leucine, alanine, phenylalanine, valine, isoleucine, glycine, serine, glutamine, glutamate and arginine do. More preferably, no other amino acids other than those listed above are present. Most preferred amino acids are those which show high activity against both S. aureus (L _s is at least about 5) and E. coli (L _e is at least about 4), which have a sequence consisting of .

(MB_00) SEQ ID NO: 1 LKLLKKLLKKLKKLL,

(MB_18) SEQ ID NO: 2 LKALKKLAKKKLKKLA,

(MB_21) SEQ ID NO: 3 FASLLGKALKALAKQ,

(MB_36) SEQ ID NO: 4 FASLLGKALKALLAKLAKQ,

(MB_37) SEQ ID NO: 5 FASLLGKLAKKLAKKALK,

(CM_1) SEQ ID NO: 7 LALLKVLLRKIKKAL,

(CM_3) SEQ ID NO: 8 ALKAALLAILKIVRVIKK.

Where L = leucine, A = alanine, F = phenylalanine, V = valine, I = isoleucine, G = glycine, K = lysine, S = serine, E = glutamate, Q = glutamine and R = arginine.

Preferably the peptide is not a homopolymer of an oligomer consisting of 3-5 amino acid residues.

The invention also provides antimicrobial (preferably antimicrobial or antifungal) compositions of matter comprising one or more peptides of the invention and in combination with other antimicrobial materials and treatments (including applying heat or pressure). ) And its use as a composition. The aforementioned compositions have found utility in sterilization, anti-corruption, preservation and other sanitary processes. It will be apparent to the skilled investigator that the peptides of the present invention will be applied in many situations that require the sterilization of bacteria or fungi.

According to another aspect of the invention, there is a method for surface sterilization, comprising the step of treating a surface with a composition consisting of a peptide according to any one of claims 1-4.

While the peptides disclosed in this application have been synthesized ex vivo by Merifield's stepwise method, it is contemplated that the peptides can be produced in vivo by using nucleic acid molecules capable of directing the synthesis of the peptides. It is within the scope of the art to produce DNA molecules encoding peptides disclosed herein and to introduce such DNA molecules into cells such that the cells can produce peptides or precursors thereof as metabolic products.

BRIEF DESCRIPTION OF THE DRAWINGS In order that the present invention may be better understood, the following description will be made with reference to the accompanying drawings.

1: SAS / RGSYS (TM) on dimensions corresponding to total charge, hydrophilic / lipophilic balance (HLB), hydrophobic moment (as described above) and amphipathic (as described above) of the peptide Vector analysis method (internal unfolding).

The peptides shown in Table 2 below were prepared by Merrifield solid phase synthesis [Al. ratio. Merifield, J. Am. Chem. Soc. (1963) Vol. 85, page 2149].

The actual bacterial activity of these peptides was found in Gram-negative bacteria (Escherichia coli ATCC 11229) and Gram-positive bacteria (Staphylococcus aureus) cultured overnight in nutrient broth (Oxoid (TM) Nr. 2). ATCC 6538), both using a total probiotic counting technique. The cells were harvested and suspended in Ringer's solution to obtain an initial cell number of 10 ⁶ -10 ⁸ . Cells were incubated with peptides aseptically in 96-well microtiter plates and placed the relevant controls. The concentration of peptide was 0.1-1 mg / ml. In both bacteria (E. coli and S. aureus), log sterilization values were determined. The measured log sterilization values are shown in Table 2 below.

Method of SAS / RGSYS (TM) vector analysis on dimensions corresponding to total charge, hydrophilic / lipophilic balance (HLB), hydrophobic moment (as described above) and amphipathic (as described above) of peptides The results were analyzed by (internal unfold). This analysis showed that these variables could be used to predict which multiple peptides would be effective antimicrobial. The results are shown in FIG. In Figure 1, AMP is amphiphilic, EC is log sterilization value for E. coli, STPH is log sterilization value for S. aureus, HM is hydrophobic moment, CH is total positive charge and HLB is hydrophilic / fat-affinity Balance.

Table 2 below shows the correlation between measured log sterilization values (expressed as acts) and predicted log sterilization values (expressed as frees) for E. coli and S. aureus for the listed peptides. The predicted value was determined by the equation provided by the present invention. It can be seen that the predicted and measured values agree very well. Peptides with a predictive log sterilization value of at least 5 for S. aureus or at least 4 log sterilization values for E. coli are examples of the invention, other examples are compared, and relatively small changes in the structure Can have significant consequences for antimicrobial activity.

Samples identified by the code MB_nn (SEQ ID NO) were peptides identified as antimicrobial as possible without reference to the predictive equation provided by the present invention. The sample identified by the code MC_nn (SEQ ID NO:) was a peptide whose sequence showed high predictive activity. These molecules were synthesized using the Merrifield solid phase synthesis method and the actual activity of the molecules against S. aureus was determined. It can be seen that there is a good correlation between the predicted and measured values of these molecules. Computer-assisted methods were used to reach the sequences of the CM-n (SEQ ID NO) series in the Examples. It can be seen among these that there is also a high correlation between the antimicrobial activity expected and the antimicrobial activity expected.

Name of Invention: Amphiphilic Peptides and Analogs thereof

Number of sequences: 13

Information about sequence number One

Sequence feature:

Length: 15 amino acids

Type: Amino Acid

Form: Linear

Molecular Type: Protein

Sequence Description: SEQ ID NO: One

Information about sequence number 2

Sequence feature:

Length: 16 amino acids

Type: Amino Acid

Form: Linear

Molecular Type: Protein

Sequence Description: SEQ ID NO: 2

Information about sequence number 3

Sequence feature:

Length: 15 amino acids

Type: Amino Acid

Form: Linear

Molecular Type: Protein

Sequence Description: SEQ ID NO: 3

Information about sequence number 4

Sequence feature:

Length: 19 amino acids

Type: Amino Acid

Form: Linear

Molecular Type: Protein

Sequence Description: SEQ ID NO: 4

Information about sequence number 5

Sequence feature:

Length: 18 amino acids

Type: Amino Acid

Form: Linear

Molecular Type: Protein

Sequence Description: SEQ ID NO: 5

Information about sequence number 6

Sequence feature:

Length: 18 amino acids

Type: Amino Acid

Form: Linear

Molecular Type: Protein

Sequence Description: SEQ ID NO: 6

Information about sequence number 7

Sequence feature:

Length: 15 amino acids

Type: Amino Acid

Form: Linear

Molecular Type: Protein

Sequence Description: SEQ ID NO: 7

Information about sequence number 8

Sequence feature:

Length: 18 amino acids

Type: Amino Acid

Form: Linear

Molecular Type: Protein

Sequence Description: SEQ ID NO: 8

Information about sequence number 9

Sequence feature:

Length: 20 amino acids

Type: Amino Acid

Form: Linear

Molecular Type: Protein

Sequence Description: SEQ ID NO: 9

Information about sequence number 10

Sequence feature:

Length: 16 amino acids

Type: Amino Acid

Form: Linear

Molecular Type: Protein

Sequence Description: SEQ ID NO: 10

Information about sequence number 11

Sequence feature:

Length: 16 amino acids

Type: Amino Acid

Form: Linear

Molecular Type: Protein

Sequence Description: SEQ ID NO: 11

Information about sequence number 12

Sequence feature:

Length: 18 amino acids

Type: Amino Acid

Form: Linear

Molecular Type: Protein

Sequence Description: SEQ ID NO: 12

Information about sequence number 13

Sequence feature:

Length: 20 amino acids

Type: Amino Acid

Form: Linear

Molecular Type: Protein

Sequence Description: SEQ ID NO: 13

Claims (5)

Amphiphilic antimicrobial peptides consisting of sequences selected from the following groups. +-++-++-+-++, +-++-++ --- +-++, ++-+++-++-+++-, ++-+++-++-++++-++-, ++-+++-++-++-++-, -++-++-++-++-++, ++++-+++-+-++, ++-+++++++-++-++-, ++-++-++-++-++-++, ++-++-++-++-++, ++-+-++-++-++, -++ --- ++-++-++-++, and ++-++-+-++-++-++. In the above, + denotes a hydrophobic amino acid residue and-denotes a hydrophilic amino acid residue. The peptide of claim 1 having a sequence selected from the group: SEQ ID NO: 1 LKLLKKLLKKLKKLL, SEQ ID NO: 2 LKALKKLAKKKLKKLA, SEQ ID NO: 3 FASLLGKALKALAKQ, SEQ ID NO: 4 FASLLGKALKALLAKLAKQ, SEQ ID NO: 5 FASLLGKLAKKLAKKALK, SEQ ID NO: 6 QKAASRLLRALSKLLEAF, SEQ ID NO: 7 LALLKVLLRKIKKAL, SEQ ID NO: 8 ALKAALLAILKIVRVIKK, SEQ ID NO: 9 AASKAAKTLAKLLSSLLKLL, SEQ ID NO: 10 LLKKLLRAASKALSLL, SEQ ID NO: 11 AAKKLSKLLKTLLKLL, SEQ ID NO: 12 KALKKKLLKLASSKKTAL, SEQ ID NO: 13 AASKALRTASRLARSLLTLL. Among the above sequences, L = leucine, A = alanine, F = phenylalanine, V = valine, I = isoleucine, G = glycine, K = lysine, S = serine, E = glutamate, Q = glutamine, T = threonine and R Arginine. The predicted log sterilization value (L _{S aureus} ) for _{S. aureus} ATCC 6538 is greater than 5 and L _{S aureus is obtained} by the equation L _{S aureus} = y [25] * (4.8362068) + (3.5316215). Antimicrobial peptide having a length of 30 amino acid residues. In the above formula, In the above formula, z ₁ = sum of hydrophobic and hydrophilic values z ₂ = Y component of the charge dipole z ₃ = sum of negative charges z ₄ = Approximate value for sine curve z ₅ = X component of the charge dipole z ₆ = Approximate fit to square curve 10-30, the predicted log sterilization value (L _{E coli} ) for E. coli ATCC 11229 is greater than 4 and L _{E coli is obtained} by the equation L _{E coli} = y [27] * (4.41875) + (3.615) An antimicrobial peptide having a length of amino acid residues. In the above formula, z ₀ is L _{S aureus} , z ₁ is the molecular weight, z ₂ is the modulus of the hydrophobic dipole moment in the Z-plane, z ₃ is a hydrophobic solvent accessible surface, z ₄ is the number of atoms greater than 8 μs from the alpha helix axis, z ₅ is the 2D diameter (R _xy ) of the gyration A method for surface sterilization comprising treating a surface with a composition consisting of the peptide according to any one of claims 1 to 4.