Peptide name : NK-pro (Derived from NK-2)

Source/Organism : Synthetic construct

Linear/Cyclic : Linear

Chirality : L

Peptide length: 27

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information: None

Assay type : MTT assay

Assay time : 24h

Activity : IC50 : 26.1 μM

Cell line : HL-60

Cancer type : Not found

Other activity : Anti-bacterial activity

Amino acid composition bar chart :

Molecular mass : 3199.0252 Dalton

Aliphatic index : 1.118

Instability index : 55.1296

Hydrophobicity (GRAVY) : -0.296

Isoelectric point : 11.604

Charge (pH 7) : 8.7453

Aromaticity : 0.037

Molar extinction coefficient (cysteine, cystine): (0, 0)

Hydrophobic/hydrophilic ratio : 1.07692307

hydrophobic moment : -0.760

Missing amino acid : W,H,Q,E,Y,N,A

Most occurring amino acid : K

Most occurring amino acid frequency : 6

Least occurring amino acid : V

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.3, 0.1, 0.3)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCSC)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@@H](N)CCCCN)[C@@H](C)CC)C(C)C)[C@@H](C)CC)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)O)[C@@H](C)O)[C@@H](C)CC

1 : Yan J, et al. Influence of Proline Substitution on the Bioactivity of Mammalian-Derived Antimicrobial Peptide NK-2. Probiotics Antimicrob Proteins. 2018; 10:118-127. doi: 10.1007/s12602-017-9335-1

Paper title : Influence of Proline Substitution on the Bioactivity of Mammalian-Derived Antimicrobial Peptide NK-2.

Doi : https://doi.org/10.1007/s12602-017-9335-1

Abstract : Multidrug-resistant bacteria are emerging as a global threat, making the search for alternative compounds urgent. Antimicrobial peptides (AMPs) became a promising hotspot due to their distinct action mechanism and possibility to be used as an alternative or complement to traditional antibiotics. However, gaining a better understanding about the relationship between antimicrobial peptides structure and its bioactivity is crucial for the development of next generation of antimicrobial agents. NK-2, derived from mammalian protein NK-lysin, has potent antitumor and bactericidal abilities. As proline was considered to be an effective α-helix breaker due to its restricted conformation, to better comprehend the effects of proline in the structure-activity relationship of NK-2, we constructed two NK-2 analogs. We examined the biological activities of NK-2 and its proline substitution analogs and analyzed the resulting conformational changes. Our results showed that introducing proline into the primary sequence of NK-2 significantly decreased the antitumor, antibacterial, and cytotoxic effects, as well as DNA binding activity by changing the α-helix content. However, α-helical content was not the only determining factor, the position of proline inserted was also critical. This study will allow for clearer insight into the role of proline in structure and bioactivity of NK-2 and provide a foundation for future studies.