Peptide name : MP1-Q12K

Source/Organism : Analog of Polybia MP1

Linear/Cyclic : Linear

Chirality : L

Peptide length: 14

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information:

Assay type : MTT assay

Assay time : 24-h

Activity : IC50 = 12.5 μM

Cell line : A-549

Cancer type : Lung Cancer

Other activity : Antimicrobial

Amino acid composition bar chart :

Molecular mass : 1640.0183 Dalton

Aliphatic index : 1.814

Instability index : 10.9143

Hydrophobicity (GRAVY) : 0.5857

Isoelectric point : 8.4975

Charge (pH 7) : 0.7593

Aromaticity : 7.142

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

Hydrophobic/hydrophilic ratio : 1.8

hydrophobic moment : -0.774

Missing amino acid : C,E,F,G,H,M,N,P,Q,R,S,T,V,Y

Most occurring amino acid : L

Most occurring amino acid frequency : 4

Least occurring amino acid : W

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (64., 14., 50)

SMILES Notation: CC[C@H](C)[C@H](N)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)O)[C@@H](C)CC

1 : Phuong HBT, et al. Effect of substituting glutamine with lysine on structural and biological properties of antimicrobial peptide Polybia-MP1. Amino Acids. 2023; 55:881-890. doi: 10.1007/s00726-023-03276-3

Paper title : Effect of substituting glutamine with lysine on structural and biological properties of antimicrobial peptide Polybia-MP1.

Doi : https://doi.org/10.1007/s00726-023-03276-3

Abstract : The natural antimicrobial peptide Polybia-MP1 is a promising candidate for developing new treatment therapy for infection and cancer. It showed broad-spectrum antimicrobial and anticancer activity with high safety on healthy cells. However, previous sequence modification usually resulted in at least one of two consequences: a notable increase in hemolytic activity or a considerable decrease in activity against Gram-negative bacteria and cancer cells. Herein, a new approach was applied by replacing the amino acid Glutamine at position 12 with Lysine and generating the MP1-Q12K analog. Our preliminary data suggested an enhancement in antibacterial and antifungal activity, whereas the anticancer and hemolytic activity of the two peptides were comparable. Moreover, MP1-Q12K was found to be less self-assembly than Polybia-MP1, which further supports the enhancement of antimicrobial properties. Hence, this study provides new information regarding the structure-activity relationships of Polybia-MP1 and support for the development of potent, selective antimicrobial peptides.