118231-04-2 Usage
General Description
Tachyplesin is a type of bioactive peptide derived from an amino acid sequence present in the hemocytes of limulus, also known as the horseshoe crab. It is a potent antimicrobial agent due to the action of the positive charge on its surface which interacts with the negatively charged surface of bacterial cells. This interaction disrupts the membrane integrity of the bacteria and induces cell lysis, thus acting as a bactericidal agent. Tachyplesin has shown high efficacy against gram-positive, gram-negative bacteria, and certain types of fungi, making it a potential candidate for therapeutic applications. Additionally, studies show that tachyplesin has antiviral and anticancer properties.
Check Digit Verification of cas no
The CAS Registry Mumber 118231-04-2 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,1,8,2,3 and 1 respectively; the second part has 2 digits, 0 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 118231-04:
(8*1)+(7*1)+(6*8)+(5*2)+(4*3)+(3*1)+(2*0)+(1*4)=92
92 % 10 = 2
So 118231-04-2 is a valid CAS Registry Number.
InChI:InChI=1/C99H151N35O19S4/c1-5-53(4)78-94(153)132-75-51-157-156-50-74(91(150)127-69(43-55-28-32-58(135)33-29-55)85(144)121-64(24-14-38-114-96(105)106)81(140)119-47-76(137)133-78)131-93(152)77(52(2)3)134-84(143)67(27-17-41-117-99(111)112)124-86(145)68(42-54-18-7-6-8-19-54)126-90(149)73(130-88(147)71(125-80(139)61(101)21-11-12-36-100)45-57-46-118-62-22-10-9-20-60(57)62)49-155-154-48-72(89(148)120-63(79(102)138)23-13-37-113-95(103)104)129-83(142)66(26-16-40-116-98(109)110)122-82(141)65(25-15-39-115-97(107)108)123-87(146)70(128-92(75)151)44-56-30-34-59(136)35-31-56/h6-10,18-20,22,28-35,46,52-53,61,63-75,77-78,118,135-136H,5,11-17,21,23-27,36-45,47-51,100-101H2,1-4H3,(H2,102,138)(H,119,140)(H,120,148)(H,121,144)(H,122,141)(H,123,146)(H,124,145)(H,125,139)(H,126,149)(H,127,150)(H,128,151)(H,129,142)(H,130,147)(H,131,152)(H,132,153)(H,133,137)(H,134,143)(H4,103,104,113)(H4,105,106,114)(H4,107,108,115)(H4,109,110,116)(H4,111,112,117)/t53-,61-,63-,64-,65-,66-,67-,68-,69-,70-,71-,72-,73-,74-,75-,77-,78-/m0/s1
118231-04-2Relevant articles and documents
Structure-Activity and a'Toxicity Relationships of the Antimicrobial Peptide Tachyplesin-1
Edwards, Ingrid A.,Elliott, Alysha G.,Kavanagh, Angela M.,Blaskovich, Mark A. T.,Cooper, Matthew A.
, p. 917 - 926 (2017)
Tachyplesin-1 (TP1; 1) is a cationic β-hairpin antimicrobial peptide with a membranolytic mechanism of action. While it possesses broad-spectrum, potent antimicrobial activity, 1 is highly hemolytic against mammalian erythrocytes, which precludes it from further development. In this study, we report a template-based approach to investigate the structure-function and structure-toxicity relationships of each amino acid of 1. We modulated charge and hydrophobicity by residue modification and truncation of the peptide. Antimicrobial activity was then assessed against six key bacterial pathogens and two fungi, with toxicity profiled against mammalian cells. The internal disulfide bridge Cys7-Cys12 of 1 was shown to play an important role in broad-spectrum antimicrobial activity against all pathogenic strains tested. Novel peptides based on the progenitor were then designed, including 5 (TP1[F4A]), 12 (TP1[I11A]), and 19 (TP1[C3A,C16A]). These had 26-to 64-fold improved activity/toxicity indices and show promise for further development. Structural studies of 5 (TP1[F4A]) and 12 (TP1[I11A]) identified a conserved β-hairpin secondary structure motif correlating with their very high stablility in mouse and human plasma. Membrane binding affinity determined by surface plasmon resonance confirmed their selectivity toward bacterial membranes, but the degree of membrane binding did not correlate with the degree of hemolysis, suggesting that other factors may drive toxicity.
