The folding dynamics and structural characteristics of peptides RTKAWNRQLYPEW （P1） and RTKQLYPEW （P2） are investigated by using all-atomic simulation procedure CHARMM in this work. The results show that P1, a segm...The folding dynamics and structural characteristics of peptides RTKAWNRQLYPEW （P1） and RTKQLYPEW （P2） are investigated by using all-atomic simulation procedure CHARMM in this work. The results show that P1, a segment of an antigen, has a folding motif of α-helix, whereas P2, which is derived by deleting four residues AWNR from peptide P1, prevents the formation of helix and presents a β-strand. And peptlde P1 experiences a more rugged energy landscape than peptide P2. From our results, it is inferred that the antibody CD8 cytolytic T lymphocyte prefers an antigen with a β-folding structure to that with an α-helical one.展开更多
The creation of artificial enzymes to mimic natural enzymes remains a great challenge owing to the complexity of the structural arrangement of the essential amino acids in catalytic centers.In this study,we used the p...The creation of artificial enzymes to mimic natural enzymes remains a great challenge owing to the complexity of the structural arrangement of the essential amino acids in catalytic centers.In this study,we used the phosphatase-based enzyme-instructed self-assembly(EISA)to supervise artificial esterases'final structures and catalytic activities.We reported that peptide precursors containing different phosphorylation sites could preorganize into alternated nanostructures and undergo dephosphorylation in the presence of alkaline phosphatase(ALP)with variation in kinetic and thermodynamic profiles.Although identical self-assembly compositions were formed after dephosphorylation,precursors with more enhanced preorganized states tended to better promote ALP dephosphorylation,facilitate further self-assembly,and strengthen the catalytic activities of the final assemblies.We envisioned that our strategy would be useful for further construction and manipulation of various artificial enzymes with superior catalytic activities.展开更多
基金Project supported by the National Natural Science Foundation of China （Grant Nos 90103031, 10474041, 90403120 and 10021001）, and the Nonlinear Project （973） of the NSM.
文摘The folding dynamics and structural characteristics of peptides RTKAWNRQLYPEW （P1） and RTKQLYPEW （P2） are investigated by using all-atomic simulation procedure CHARMM in this work. The results show that P1, a segment of an antigen, has a folding motif of α-helix, whereas P2, which is derived by deleting four residues AWNR from peptide P1, prevents the formation of helix and presents a β-strand. And peptlde P1 experiences a more rugged energy landscape than peptide P2. From our results, it is inferred that the antibody CD8 cytolytic T lymphocyte prefers an antigen with a β-folding structure to that with an α-helical one.
基金supported by the National Science Fund for Distinguished Young Scholars(31825012)the National Natural Science Foundation of China(21875116,31961143004,81921004)+1 种基金the National Key Research and Development Program of China(2017YFC1103502,2018YFC1003401)the China Postdoctoral Science Foundation(2020M680856)。
文摘The creation of artificial enzymes to mimic natural enzymes remains a great challenge owing to the complexity of the structural arrangement of the essential amino acids in catalytic centers.In this study,we used the phosphatase-based enzyme-instructed self-assembly(EISA)to supervise artificial esterases'final structures and catalytic activities.We reported that peptide precursors containing different phosphorylation sites could preorganize into alternated nanostructures and undergo dephosphorylation in the presence of alkaline phosphatase(ALP)with variation in kinetic and thermodynamic profiles.Although identical self-assembly compositions were formed after dephosphorylation,precursors with more enhanced preorganized states tended to better promote ALP dephosphorylation,facilitate further self-assembly,and strengthen the catalytic activities of the final assemblies.We envisioned that our strategy would be useful for further construction and manipulation of various artificial enzymes with superior catalytic activities.
