Peptide name : MPC-A5K,A8K

Source/Organism : Amino acid substitution

Linear/Cyclic : Not found

Chirality : Not found

Peptide length: 14

C-terminal modification: Not found

N-terminal modification : Not found

Non-natural peptide information: None

Assay type : Not specified

Assay time : Not found

Activity : Not found

Cell line : Not found

Cancer type : Not found

Other activity : Anti-microbial activity

Amino acid composition bar chart :

Molecular mass : 1622.1339 Dalton

Aliphatic index : 1.95

Instability index : -7.2786

Hydrophobicity (GRAVY) : 0.4643

Isoelectric point : 10.602

Charge (pH 7) : 4.7551

Aromaticity : 0

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

Hydrophobic/hydrophilic ratio : 1.33333333

hydrophobic moment : -1.653

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

Most occurring amino acid : L

Most occurring amino acid frequency : 5

Least occurring amino acid : N

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.7, 0.0, 0.5)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](N)CC(C)C)C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)O

1 : Thi Phuong HB, et al. Reducing Self-Assembly by Increasing Net Charge: Effect on Biological Activity of Mastoparan C. ACS Med Chem Lett. 2024; 15:69-75. doi: 10.1021/acsmedchemlett.3c00385

Paper title : Reducing Self-Assembly by Increasing Net Charge: Effect on Biological Activity of Mastoparan C.

Doi : https://doi.org/10.1021/acsmedchemlett.3c00385

Abstract : The ability of amphipathic peptides to arrange themselves in aqueous solutions, known as self-assembly, has been found to reduce the effectiveness of these peptides in interacting with cell membranes. Therefore, minimizing their tendency to self-assemble could be a potential strategy for enhancing the pharmacological properties of antimicrobial peptides (AMPs). To explore this idea, this study prepared a series of natural peptides mastoparan C (MPC) with increased net charge and hydrophilicity via alanine-to-lysine substitution and investigated the impact on the biological activity. The preliminary data suggested the influence of both the overall positive charge and the position of a lysine residue on the self-assembly of MPC and its derivatives. Besides, the analogue MPC-A5K,A8K displayed higher anticancer activity and comparable antimicrobial activity with significantly lower hemolysis than MPC. Hence, reducing self-assembly by expanding the cationic area could be a promising approach for developing potent and selective AMPs.