Skip to Content
Merck
All Photos(3)

Documents

G5002

Sigma-Aldrich

Gramicidin

from Bacillus aneurinolyticus (Bacillus brevis), powder or crystalline powder, antibiotic

Sign Into View Organizational & Contract Pricing
All Photos(3)

About This Item

CAS Number:
1405-97-6
EC Number:
215-790-4
MDL number:
MFCD00131232
UNSPSC Code:
12161501
NACRES:
NA.77

product name

Gramicidin from Bacillus aneurinolyticus (Bacillus brevis), Linear polypeptide antibiotic complex. A mixture of gramicidins A, B, C, and D.

Quality Level

200

antibiotic activity spectrum

Gram-negative bacteria
Gram-positive bacteria

Mode of action

cell membrane | interferes
enzyme | inhibits

storage temp.

2-8°C

InChI

1S/C99H140N20O17/c1-51(2)37-73(109-86(123)59(17)107-81(122)49-105-96(133)82(55(9)10)106-50-121)89(126)108-60(18)87(124)117-84(57(13)14)98(135)119-85(58(15)16)99(136)118-83(56(11)12)97(134)116-80(44-64-48-104-72-34-26-22-30-68(64)72)95(132)112-76(40-54(7)8)92(129)115-79(43-63-47-103-71-33-25-21-29-67(63)71)94(131)111-75(39-53(5)6)91(128)114-78(42-62-46-102-70-32-24-20-28-66(62)70)93(130)110-74(38-52(3)4)90(127)113-77(88(125)100-35-36-120)41-61-45-101-69-31-23-19-27-65(61)69/h19-34,45-48,50-60,73-80,82-85,101-104,120H,35-44,49H2,1-18H3,(H,100,125)(H,105,133)(H,106,121)(H,107,122)(H,108,126)(H,109,123)(H,110,130)(H,111,131)(H,112,132)(H,113,127)(H,114,128)(H,115,129)(H,116,134)(H,117,124)(H,118,136)(H,119,135)/t59-,60-,73+,74+,75+,76+,77-,78-,79-,80-,82-,83-,84+,85-/m0/s1

InChI key

ZWCXYZRRTRDGQE-SORVKSEFSA-N

General description

Chemical structure: peptide
Gramicidin A is a linear pentadecapeptide antibiotic produced by Bacillus brevis. The transmembrane protein contains a left-handed helix with alternating L and D residues.

Application

Gramicidin from Bacillus aneurinolyticus (Bacillus brevis) has been used as a control to measure the rate of diffusion of protonated β-lactams through the lipid bilayer in liposome swelling assay. It has also been used as an analyte for the purpose of infrared laser desorption or ionization from silicon.

Biochem/physiol Actions

Linear polypeptide antibiotic mixture of gramicidin A, B, C, and D. Gramicidin A acts as neutral carrier and helps in the establishment of ion flux across the lipid bilayer.
Linear polypeptide antibiotic, a mixture of gramicidin A, B, C, and D. Gramicidin D, a channel-forming ionophore that flip-flops slowly across the membrane is a known Pgp substrate and surprisingly was found to inhibit Pgp ATPase activity. This inhibition was reversed by other Pgp substrates suggesting a common drug binding site among MDR substrate-type drugs and chemosensitizers.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Infrared laser desorption/ionization on silicon.
Bhattacharya S H, et al.
Analytical Chemistry, 74(9), 2228-2231 (2002)
Porin channels in Escherichia coli: studies with liposomes reconstituted from purified proteins.
Nikaido H and Rosenberg E Y
Journal of Bacteriology, 153(1), 241-252 (1983)
E J Prenner et al.
Biochimica et biophysica acta, 1462(1-2), 201-221 (1999-12-11)
Gramicidin S (GS) is a cyclic decapeptide of primary structure [cyclo-(Val-Orn-Leu-D-Phe-Pro)(2)] secreted by Bacillus brevis. It is a powerful antimicrobial agent with potent cidal action on a wide variety of Gram-negative and Gram-positive bacteria as well as on several pathogenic
Jens A Lundbaek et al.
Journal of the Royal Society, Interface, 7(44), 373-395 (2009-11-27)
Membrane protein function is regulated by the host lipid bilayer composition. This regulation may depend on specific chemical interactions between proteins and individual molecules in the bilayer, as well as on non-specific interactions between proteins and the bilayer behaving as
Rong Chen et al.
Toxins, 5(2), 456-471 (2013-02-26)
Various gating modifier toxins partition into membranes and interfere with the gating mechanisms of biological ion channels. For example, GsMTx4 potentiates gramicidin and several bacterial mechanosensitive channels whose gating kinetics are sensitive to mechanical properties of the membrane, whereas binding
View All Related Papers

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service