»ã±¨±êÌâ (Title)£ºDissecting the Mechanism of Polypeptide Pathological Aggregation and Functional Self-assembly : Molecular Simulation Studies£¨»ùÓÚ·Ö×Ó¶¯Á¦Ñ§·ÂÕÕ̽Ë÷µ°°×ÖʶàëIJ¡ÀíÐÔÜöÝͺÍÖ°ÄÜÐÔ×Ô×é×°·Ö×Ó»úÀí£©

»ã±¨ÈË (Speaker)£ºËïÔËÏé ¸±½ÌÊÚ£¨Äþ²¨´óѧ£©

»ã±¨¹¦·ò (Time)£º2022Äê11ÔÂ18ÈÕ (ÖÜÎå) 10:00-12:00

»ã±¨µØÖ· (Place)£ºÌÚѶ»áÒ飨»áÒéºÅ£º800-918-782£©

Ô¼ÇëÈË(Inviter)£ºÁõºÃºº ½ÌÊÚ

Ö÷°ì²¿ÃÅ£ºÀíѧԺÎïÀíϵ

»ã±¨ÌáÒª£ºThe spontaneous self-assembly of polypeptides into amyloid fibrils has attracted extensive attention due to their association with numerous human degenerative diseases, physiological functions, and potential applications in biomedicine and bio-nanotechnology. Soluble low-molecular-weight oligomers formed during the early aggregation of amyloid peptides have been hypothesized as a major toxic species of amyloidogenesis. However, oligomers formed during the assembly process are usually heterogeneous and unstable, making their isolation, quantification, and structural determination experimentally challenging. Characterization of these oligomeric intermediates is helpful for both understanding the pathogenesis and anti-amyloidosis drug design, which also aids in the functional amyloid peptides design. In my presentation, I will discuss the self-assembly mechanism of the disease-related polypeptide as well as the functional amyloid peptides based on our prior systematically investigated the aggregation of amyloid-beta, amylin, suckerin, beta-endorphin peptides.