Peptide name : [G10a]3-SHa

Source/Organism : Analog of temporin SHa

Linear/Cyclic : Linear

Chirality : Mix

Peptide length: 41

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information:

Assay type : Resazurin dye assay

Assay time : 48-h

Activity : IC50 = 3.77 ± 0.12 µM

Cell line : MCF-7

Cancer type : Breast Cancer

Other activity : Antimicrobial and Anticancer

Amino acid composition bar chart :

Molecular mass : 4407.5652 Dalton

Aliphatic index : 1.353

Instability index : -18.758

Hydrophobicity (GRAVY) : 1.5585

Isoelectric point : 10.602

Charge (pH 7) : 4.7551

Aromaticity : 14.63

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

Hydrophobic/hydrophilic ratio : 3.75

hydrophobic moment : -0.225

Missing amino acid : A,C,D,E,H,N,P,Q,R,T,W,Y

Most occurring amino acid : L

Most occurring amino acid frequency : 9

Least occurring amino acid : S

Least occurring amino acid frequency : 3

Secondary structure fraction (Helix, Turn, Sheet): (48., 21., 51.)

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

1 : Khan AI, et al. Design, Synthesis and Characterization of [G10a]-Temporin SHa Dendrimers as Dual Inhibitors of Cancer and Pathogenic Microbes. Biomolecules. 2022; 12:(unknown pages). doi: 10.3390/biom12060770

Paper title : Design, Synthesis and Characterization of [G10a]-Temporin SHa Dendrimers as Dual Inhibitors of Cancer and Pathogenic Microbes.

Doi : https://doi.org/10.3390/biom12060770

Abstract : As the technologies for peptide synthesis and development continue to mature, antimicrobial peptides (AMPs) are being widely studied as significant contributors in medicinal chemistry research. Furthermore, the advancement in the synthesis of dendrimers' design makes dendrimers wonderful nanostructures with distinguishing properties. This study foregrounds a temporin SHa analog, [G10a]-SHa, and its dendrimers as globular macromolecules possessing anticancer and antibacterial activities. These architectures of temporin SHa, named as [G10a]-SHa, its dendrimeric analogs [G10a]₂-SHa and [G10a]₃-SHa, and [G10a]₂-SHa conjugated with a polymer molecule, i.e., Jeff-[G10a]₂-SHa, were synthesized, purified on RP-HPLC and UPLC and fully characterized by mass, NMR spectroscopic techniques, circular dichroism, ultraviolet, infrared, dynamic light scattering, and atomic force microscopic studies. In pH- and temperature-dependent studies, all of the peptide dendrimers were found to be stable in the temperature range up to 40-60 °C and pH values in the range of 6-12. Biological-activity studies showed these peptide dendrimers possessed improved antibacterial activity against different strains of both Gram-positive and Gram-negative strains. Together, these dendrimers also possessed potent selective antiproliferative activity against human cancer cells originating from different organs (breast, lung, prostate, pancreas, and liver). The high hemolytic activity of [G10a]₂-SHa and [G10a]₃-SHa dendrimers, however, limits their use for topical treatment, such as in the case of skin infection. On the contrary, the antibacterial and anticancer activities of Jeff-[G10a]₂-SHa, associated with its low hemolytic action, make it potentially suitable for systemic treatment.