AMPDB_716 | Dermaseptin-S1

1 General Description

AMPDB ID: AMPDB_716

Protein Names: Dermaseptin-S1 (DRS-S1) (Dermaseptin) (DS) (Dermaseptin I) (DS I) (Dermaseptin-1) (DS1)

Protein Family: Frog skin active peptide (FSAP) family; Dermaseptin subfamily

Gene Name: Nil

Source Organism: Phyllomedusa sauvagei (Sauvage`s leaf frog)

Protein Length: 79 AA

Protein Existence: Evidence at protein level

2 Protein Sequence & Composition

MDILKKSLFLVLFLGLVSLSICEEEKRENEDEEKQEDDEQSEMKRALWKTMLKKLGTMALHAGKAALGAAADTISQGTQ

FASTA format

Counts of Amino Acids

'A': 8, 'R': 2, 'N': 1, 'D': 5, 'C': 1, 'Q': 4, 'E': 10, 'G': 5, 'H': 1, 'I': 3, 'L': 12, 'K': 9, 'M': 4, 'F': 2, 'P': 0, 'S': 5, 'T': 4, 'W': 1, 'Y': 0, 'V': 2

Frequencies of Amino Acids

'A': 10.13%, 'R': 2.53%, 'N': 1.27%, 'D': 6.33%, 'C': 1.27%, 'Q': 5.06%, 'E': 12.66%, 'G': 6.33%, 'H': 1.27%, 'I': 3.8%, 'L': 15.19%, 'K': 11.39%, 'M': 5.06%, 'F': 2.53%, 'P': 0%, 'S': 6.33%, 'T': 5.06%, 'W': 1.27%, 'Y': 0%, 'V': 2.53%

Missing Amino Acid(s)

P, Y

Most Occurring Amino Acid(s)

Less Occurring Amino Acid(s)

C, H, N, W

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	8812.16 Da	Computed by ProtParam module (biopython 1.79)
2.	Aliphatic Index	91.519	Computed by ProtParam module (biopython 1.79)
3.	Instability Index (Half Life)	49.237	Computed by ProtParam module (biopython 1.79)
4.	Hydrophobicity (GRAVY)	-0.372	Computed by ProtParam module (biopython 1.79)
5.	Hydrophobic Moment	0.509	Computed by ProtParam module (biopython 1.79)
6.	Isoelectric Point	4.654	Computed by ProtParam module (biopython 1.79)
7.	Charge (at pH 7)	-3.956	Computed by ProtParam module (biopython 1.79)
8.	Secondary Structure Fraction	0.253, 0.139, 0.43 [Helix, Turn, Sheet]	Computed by ProtParam module (biopython 1.79)
9.	Aromaticity	0.038	Computed by ProtParam module (biopython 1.79)
10.	Molar Extinction Coefficient (cysteine\|cystine)	5500, 5500	Computed by ProtParam module (biopython 1.79)

4.1 Target Organism(s)

Gram Negative Bacteria and Gram Positive Bacteria

4.2 Antimicrobial Activity

Amphibian defense peptide, Antibiotic, Antimicrobial, Antiviral protein, Fungicide, Anti-protozoal, Anti-gram-negative, Anti-gram-Positive

4.3 Enzymatic Activity

4.4 Inhibitory Effect

4.5 Other Biological Activity

Cytotoxin, Hemolytic, Spermicidal, Non-ribosomal

Activity data manually curated from Literature and UniProt

5 Database Cross-references

5.1 Literature Database

Citation 1: Chen T, Tang L, Shaw C, et al. Identification of three novel Phyllomedusa sauvagei dermaseptins (sVI-sVIII) by cloning from a skin secretion-derived cDNA library. Regul Pept. 2003;116(1-3):139-46. Published 2003 Nov 15. doi:10.1016/j.regpep.2003.08.001

PMID: 14599725

Citation 2: Mor A, Nguyen VH, Delfour A, et al. Isolation, amino acid sequence, and synthesis of dermaseptin, a novel antimicrobial peptide of amphibian skin. Biochemistry. 1991;30(36):8824-30. Published 1991 Sep 10. doi:10.1021/bi00100a014

PMID: 1909573

Citation 3: Mor A, Nicolas P, Nicolas P. Isolation and structure of novel defensive peptides from frog skin. Eur J Biochem. 1994;219(1-2):145-54. Published 1994 Jan 15. doi:10.1111/j.1432-1033.1994.tb19924.x

PMID: 8306981

Citation 4: Mor A, Nicolas P, Nicolas P. The NH2-terminal alpha-helical domain 1-18 of dermaseptin is responsible for antimicrobial activity. J Biol Chem. 1994;269(3):1934-9. Published 1994 Jan 21. doi:

PMID: 8294443

Citation 5: Ammar B, PÃ©rianin A, Mor A, et al. Dermaseptin, a peptide antibiotic, stimulates microbicidal activities of polymorphonuclear leukocytes. Biochem Biophys Res Commun. 1998;247(3):870-5. Published 1998 Jun 29. doi:10.1006/bbrc.1998.8879

PMID: 9647785

Citation 6: Chinchar VG, Bryan L, Silphadaung U, et al. Inactivation of viruses infecting ectothermic animals by amphibian and piscine antimicrobial peptides. Virology. 2004;323(2):268-75. Published 2004 Jun 1. doi:10.1016/j.virol.2004.02.029

PMID: 15193922

Citation 7: Zairi A, BelaÃ¯d A, Gahbiche A, et al. Spermicidal activity of dermaseptins. Contraception. 2005;72(6):447-53. Published 2005 Dec. doi:10.1016/j.contraception.2005.06.055

PMID: 16307969

Citation 8: VanCompernolle SE, Taylor RJ, Oswald-Richter K, et al. Antimicrobial peptides from amphibian skin potently inhibit human immunodeficiency virus infection and transfer of virus from dendritic cells to T cells. J Virol. 2005;79(18):11598-606. Published 2005 Sep. doi:10.1128/JVI.79.18.11598-11606.2005

PMID: 16140737

Citation 9: PÃ©rez-Cordero JJ, Lozano JM, CortÃ©s J, et al. Leishmanicidal activity of synthetic antimicrobial peptides in an infection model with human dendritic cells. Peptides. 2011;32(4):683-90. Published 2011 Apr. doi:10.1016/j.peptides.2011.01.011

PMID: 21262294

Citation 10: Amiche M, Ladram A, Nicolas P, et al. A consistent nomenclature of antimicrobial peptides isolated from frogs of the subfamily Phyllomedusinae. Peptides. 2008;29(11):2074-82. Published 2008 Nov. doi:10.1016/j.peptides.2008.06.017

PMID: 18644413

5.2 Protein Sequence Databases

5.3 3D Structure Databases

AlphaFoldDB: P24302

5.4 Nucleotide Sequence Databases

Sl. no.	Accession(s)	Access Link(s)
1.	AJ564794	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: IPR022731, IPR004275, IPR016322

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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