structural dynamic of a self-assembling peptide d-eak16 made of only d-amino acids结构的动态自组装肽分子d-eak16只做的酸.pdfVIP

Structural Dynamic of a Self-Assembling Peptide d-EAK16 Made of Only D-Amino Acids Zhongli Luo, Xiaojun Zhao, Shuguang Zhang* West China Hospital, Laboratory for Nanobiomedical Technology, Sichuan University, Chengdu, Sichuan, China Abstract We here report systematic study of structural dynamics of a 16-residue self-assembling peptide d-EAK16 made of only D- amino acids. We compare these results with its chiral counterpart L-form, l-EAK16. Circular dichroism was used to follow the structural dynamics under various temperature and pH conditions. At 25uC the d-EAK16 peptide displayed a typical beta- sheet spectrum. Upon increasing the temperature above 70uC, there was a spectrum shift as the 218 nm valley widens toward 210 nm. Above 80uC, the d-EAK16 peptide transformed into a typical alpha-helix CD spectrum without going through a detectable random-coil intermediate. When increasing the temperature from 4uC to 110uC then cooling back from 110uC to 4uC, there was a hysteresis: the secondary structure from beta-sheet to alpha-helix and then from alpha-helix to beta-sheet occurred. d-EAK16 formed an alpha-helical conformation at pH0.76 and pH12 but formed a beta-sheet at neutral pH. The effects of various pH conditions, ionic strength and denaturing agents were also noted. Since D-form peptides are resistant to natural enzyme degradation, such drastic structural changes may be exploited for fabricating molecular sensors to detect minute environmental changes. This provides insight into the behaviors of self-assembling peptides made of D-amino acids and points the way to designing new peptide materials for biomedical engineering and nanobiotechnology. Citation: Luo Z, Zhao X, Zhang S (2008) Structural Dynamic of a Self-Assembling Peptide d-EAK16 Made of Only D-Amino Acids