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MYP_064183
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Basic Information
Gramicidin A
Anticancer
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Antimicrobial ▸ Antibiotic activity
Antiparasitic ▸ Antimalarial
Antiparasitic ▸ General antiparasitic ▸ Antiparasitic
Antiviral
Reproductive biology ▸ Contraceptive activity ▸ Spermicidal
Wound healing/Regeneration ▸ Wound healing
Standard
15 amino acids
C96H135N19O16
Standard
Sequence
VGALAVVVWLWLWLW
Physicochemical Analysis
1811.22 Da
5.50
-0.27
-0.48
-0.0177
2.11
0.08
0.90
70.05
194.67
0.2667
22000.00
22000.00
The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.
Residue Composition
Amino Acid Composition
Chemical Descriptors
533.88
5.56
20.0
16.0
49.0
131.0
8.0
14.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0072782 VERIFIED: YES
Provenance & Taxonomy
Bacillus brevis [Bacterium]
Structure & Mods
linear peptide [Linear]
mixed L/D amino-acid peptide [Mixed]
Isolated in 1939, it is the first peptide antibiotic used clinically but it is only used topically (AMPs in use). Chemical modification: Synthesized non-ribosomally by a multienzyme complex. Both the N- and C-termini are chemically modified (CHO at the N-terminus and NHCH2CH2OH at the C-terminus). N-terminus is rich in Val, while the C-terminus is rich in Trp. Amino acids 4, 6, 8, 10, and 12 are D-amino acids. Structure in lipid bilayer: It forms a special helical structure followed by head-to-head dimerization into a cation channel in lipid bilayer with the C-terminus exposed (Ketchem RR et al 1996 J Biomol NMR 8: 1). You can rotate, zoom, and view the 3D structure here in the PDB. Structures solved in organic solvents by x-ray diffraction are believed to be non-channel forms
Bio-Activity Profile
Antimicrobial Antiviral Anticancer Spermicidal
cholangiocarcinoma cell growth through EGR4 (early growth response protein 4)
PaperSTUDIES ON A BACTERICIDAL AGENT EXTRACTED FROM A SOIL BACILLUS : I. PREPARATION OF THE AGENT. ITS ACTIVITY IN VIT
RECORD: Rec_0121186 VERIFIED: YES
Provenance & Taxonomy
Bacillus brevis [Bacterium]
Bacteriocin
Structure & Mods
topology not specified [Not included yet]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Antiviral
PaperPubMed PMID: 19870884 | PubMed PMID: 8810522 PMID19870884;8810522 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/19870884/
RECORD: Rec_0211968 VERIFIED: NO
Provenance & Taxonomy
Bacteria [Bacterium]
2
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial
RECORD: Rec_0231902 VERIFIED: YES
Provenance & Taxonomy
Bacillus brevis [Bacterium]
Bacteriocin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive
Streptococcus hemolyticus
PMID19870884 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/19870884/
RECORD: Rec_0238239 VERIFIED: YES
Provenance & Taxonomy
Brevibacillus brevis [Bacterium]
Gramicidin
1393
Structure & Mods
linear peptide [Linear]
mixed L/D amino-acid peptide [Mixed]
Ethanolamine
C-terminal ethanolamine
Bio-Activity Profile
Antibacterial Wound healing
PaperIdentification of Effective Dimeric Gramicidin-D Peptide as Antimicrobial Therapeutics over Drug Resistance: In-Silico Approach PMID30182355 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/30182355/
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