118231-04-2 Usage
Description
Tachyplesin is a bioactive peptide derived from the hemocytes of limulus, commonly known as the horseshoe crab. It is characterized by its potent antimicrobial properties, which are attributed to the positive charge on its surface that interacts with the negatively charged surface of bacterial cells, leading to membrane disruption and cell lysis. Tachyplesin exhibits high efficacy against both gram-positive and gram-negative bacteria, as well as certain fungi, and has also demonstrated antiviral and anticancer properties, making it a promising candidate for various therapeutic applications.
Uses
Used in Pharmaceutical Industry:
Tachyplesin is used as an antimicrobial agent for its high efficacy against a broad spectrum of bacteria, including gram-positive, gram-negative, and certain fungi. Its ability to disrupt bacterial cell membranes and induce cell lysis makes it a valuable component in the development of new antibiotics and antimicrobial therapies.
Used in Antiviral Applications:
Tachyplesin is used as an antiviral agent due to its demonstrated ability to inhibit viral replication and infection. Its antiviral properties can be harnessed in the development of treatments for various viral diseases, potentially offering new therapeutic options for patients.
Used in Anticancer Applications:
Tachyplesin is used as an anticancer agent, as studies have shown its potential to inhibit the growth and proliferation of cancer cells. Its anticancer properties can be utilized in the development of novel cancer therapies, providing an additional tool in the fight against various types of cancer.
Used in Cosmetics Industry:
Tachyplesin can be used as a natural preservative in cosmetics and personal care products due to its antimicrobial properties. Its ability to inhibit the growth of bacteria and fungi can help maintain the safety and shelf life of these products, while also providing a more natural and eco-friendly alternative to synthetic preservatives.
Used in Food Industry:
Tachyplesin can be used as a natural food preservative to extend the shelf life of various food products and prevent spoilage caused by bacterial and fungal contamination. Its antimicrobial properties can help maintain the freshness and quality of food items, while also offering a more natural and health-conscious alternative to synthetic preservatives.
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.
