AMPDB_64 | Amphipathic peptide CT1

1 General Description

AMPDB ID: AMPDB_64

Protein Names: Amphipathic peptide CT1 (VmCT1) (Non-disulfide-bridged peptide 4.13) (NDBP-4.13) (Non-disulfide-bridged peptide 5.13) (NDBP-5.13)

Protein Family: Non-disulfide-bridged peptide (NDBP) superfamily; Short antimicrobial peptide (group 4) family

Gene Name: Nil

Source Organism: Vaejovis mexicanus smithi (Mexican scorpion) (Vaejovis smithi)

Protein Length: 68 AA

Protein Existence: Evidence at protein level

2 Protein Sequence & Composition

MKTQFVILIVAVVLLQLISHSEAFLGALWNVAKSVFGKRGLRNFDDLDDTFEPEMSEADLKYLQDLLR

FASTA format

Counts of Amino Acids

'A': 5, 'R': 3, 'N': 2, 'D': 6, 'C': 0, 'Q': 3, 'E': 4, 'G': 3, 'H': 1, 'I': 3, 'L': 12, 'K': 4, 'M': 2, 'F': 5, 'P': 1, 'S': 4, 'T': 2, 'W': 1, 'Y': 1, 'V': 6

Frequencies of Amino Acids

'A': 7.35%, 'R': 4.41%, 'N': 2.94%, 'D': 8.82%, 'C': 0%, 'Q': 4.41%, 'E': 5.88%, 'G': 4.41%, 'H': 1.47%, 'I': 4.41%, 'L': 17.65%, 'K': 5.88%, 'M': 2.94%, 'F': 7.35%, 'P': 1.47%, 'S': 5.88%, 'T': 2.94%, 'W': 1.47%, 'Y': 1.47%, 'V': 8.82%

Missing Amino Acid(s)

Most Occurring Amino Acid(s)

Less Occurring Amino Acid(s)

H, P, W, Y

Hydrophobic Amino Acid(s) Count

Hydrophilic Amino Acid(s) Count

Basic Amino Acid(s) Count

Acidic Amino Acid(s) Count

Modified Amino Acid(s) Count

Modified Amino Acid(s) Frequencies

Computed by biopython (version 1.79) & proteinAnalysis (version 1)

3 Physicochemical Properties

Sl. No.	Properties	Values	Reference
1.	Molecular Mass	7770.04 Da	Computed by ProtParam module (biopython 1.79)
2.	Aliphatic Index	118.971	Computed by ProtParam module (biopython 1.79)
3.	Instability Index (Half Life)	49.691	Computed by ProtParam module (biopython 1.79)
4.	Hydrophobicity (GRAVY)	0.246	Computed by ProtParam module (biopython 1.79)
5.	Hydrophobic Moment	0.844	Computed by ProtParam module (biopython 1.79)
6.	Isoelectric Point	4.61	Computed by ProtParam module (biopython 1.79)
7.	Charge (at pH 7)	-2.903	Computed by ProtParam module (biopython 1.79)
8.	Secondary Structure Fraction	0.412, 0.147, 0.338 [Helix, Turn, Sheet]	Computed by ProtParam module (biopython 1.79)
9.	Aromaticity	0.103	Computed by ProtParam module (biopython 1.79)
10.	Molar Extinction Coefficient (cysteine\|cystine)	6990, 6990	Computed by ProtParam module (biopython 1.79)

4.1 Target Organism(s)

Plasmodium gallinaceum, Trypanosoma cruzi

4.2 Antimicrobial Activity

Antibiotic, Antimicrobial, Anti-parasitic, Anti-plasmodium

4.3 Enzymatic Activity

4.4 Inhibitory Effect

4.5 Other Biological Activity

Cytolysis, Anti-cancer, Cytotoxin, Hemolytic, Non-ribosomal

Activity data manually curated from Literature and UniProt

5 Database Cross-references

5.1 Literature Database

Citation 1: RamÃrez-Carreto S, Quintero-HernÃ¡ndez V, JimÃ©nez-Vargas JM, et al. Gene cloning and functional characterization of four novel antimicrobial-like peptides from scorpions of the family Vaejovidae. Peptides. 2012;34(2):290-5. Published 2012 Apr. doi:10.1016/j.peptides.2012.02.002

PMID: 22342498

Citation 2: Pedron CN, Torres MT, Lima JADS, et al. Novel designed VmCT1 analogs with increased antimicrobial activity. Eur J Med Chem. 2017;126:456-463. Published 2017 Jan 27. doi:10.1016/j.ejmech.2016.11.040

PMID: 27912176

Citation 3: Pedron CN, AraÃºjo I, da Silva Junior PI, et al. Repurposing the scorpion venom peptide VmCT1 into an active peptide against Gram-negative ESKAPE pathogens. Bioorg Chem. 2019;90:103038. Published 2019 Sep. doi:10.1016/j.bioorg.2019.103038

PMID: 31212183

Citation 4: Pedron CN, de Oliveira CS, da Silva AF, et al. The effect of lysine substitutions in the biological activities of the scorpion venom peptide VmCT1. Eur J Pharm Sci. 2019;136:104952. Published 2019 Aug 1. doi:10.1016/j.ejps.2019.06.006

PMID: 31181304

Citation 5: Pedron CN, Freire KA, Torres MT, et al. Arg-substituted VmCT1 analogs reveals promising candidate for the development of new antichagasic agent. Parasitology. 2020;147(14):1810-1818. Published 2020 Dec. doi:10.1017/S0031182020001882

PMID: 33004083

Citation 6: Pedron CN, Silva AF, Torres MT, et al. Net charge tuning modulates the antiplasmodial and anticancer properties of peptides derived from scorpion venom. J Pept Sci. 2021;27(4):e3296. Published 2021 Apr. doi:10.1002/psc.3296

PMID: 33442881

Citation 7: Zeng XC, Zhou L, Shi W, et al. Three new antimicrobial peptides from the scorpion Pandinus imperator. Peptides. 2013;45:28-34. Published 2013 Jul. doi:10.1016/j.peptides.2013.03.026

PMID: 23624072

Citation 8: Almaaytah A, Albalas Q, Albalas Q. Scorpion venom peptides with no disulfide bridges: a review. Peptides. 2014;51:35-45. Published 2014 Jan. doi:10.1016/j.peptides.2013.10.021

PMID: 24184590

5.2 Protein Sequence Databases

5.3 3D Structure Databases

AlphaFoldDB: I0DEB3

5.4 Nucleotide Sequence Databases

Sl. no.	Accession(s)	Access Link(s)
1.	JQ086325	GenBank \|\| EMBL

RefSeq: Not found

5.5 Protein-Protein Interaction Databases

STRING: Not found

IntAct: Not found

BioGRID: Not found

5.6 Ligand Databases

BindingDB: Not found

DrugBank: Not found

ChEMBL: Not found

5.7 Family & Domain Databases

InterPro: Not found

PANTHER: Not found

PROSITE: Not found

5.8 Genome Annotation Databases

Ensembl: Not found

5.9 Phylogenomic Databases

GeneTree: Not found

5.10 Enzyme & Pathway Databases

BRENDA: Not found

BioCyc: Not found

5.11 Protein-RNA Interaction Databases

RNAct: Not found

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