Development Of Thrombus Inhibitor Lernsty Targeted At Collagen
Keywords
Arterial Thrombosis,Collagen,Thrombus Inhibitor,Solubility
Abstract
By replacing the hydrophobic amino acid residue W in LWWNSYY with charged amino acid residues to optimize its composition, the thrombus inhibitor LERNSTY was designed. The study found that LERNSTY has good solubility and can effectively bind collagen, with Kd of (1.647¡À0.303) ¦Ìmol/L and effective half inhibitory concentration (IC50) of (2.73¡À0.48) ¦Ìg/mL, which is better than LWWNSYY. Therefore, the optimization of LERNSTY, an effective thrombus inhibitor, through the introduction of charged amino acids will promote the development of antithrombotic drugs with significant efficacy and few side effects. A thrombus inhibitor LERNSTY was designed based on the optimization of LWWNSYY by replacing the hydrophobic amino acid residue W with charged amino acid residues. LERNSTY was found to have good solubility. It could effectively bind with collagen with a Kd of (1.647¡À0.303) ¦Ìmol /L. An effective half inhibitory concentration (IC50) of (2.73¡À0.48) ¦Ìg/mL was obtained, which was better than that of LWWNSYY. Therefore, an effective thrombus inhibitor LERNSTY was obtained through the introduction of charged amino acid residues, which would facilitate the development of curative antithrombotic drugs with fewer side effects
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Original research was done by Zhang Lin, Hao Tanyi
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