PMC:5487955 / 12332-13760 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/5487955","sourcedb":"PMC","sourceid":"5487955","source_url":"https://www.ncbi.nlm.nih.gov/pmc/5487955","text":"4. Conclusions\nIn summary, we developed an approach for selecting cooperative peptide pairs for inhibiting enzymes on screening an array of peptides. The primary peptide inhibitor was crosslinked with enzymes to stabilize the inhibited peptide–enzyme complex. Then, secondary effect peptides were identified as only binding strongly to the inhibited peptide–enzyme complex. These secondary effect peptides also bound weakly to uninhibited enzyme on microarray, and thus had little effect on enzyme activity in solution by themselves. We validated the selected secondary effect peptides in a solution-based enzyme assay in which the combination of primary peptides and secondary effect peptides produced more inhibition on enzyme activity than that for primary peptides or secondary effect peptides alone. For negative control, we also tested a negatively-charged peptide that did not show strong binding to β-gal or crosslinked PEP-1–β-gal complex. As a result, this NEG peptide not only showed no cooperative inhibition with PEP-1, but also disrupted the inhibited PEP-1–β-gal complex, recovering enzyme activity. The selection of these cooperative or noncooperative peptide pairs may provide a versatile toolkit for modulating enzyme functions, which may find more utility in drug discovery and biocatalysis. A similar approach for searching enzyme modifiers could also be applied to small molecules that are capable of array.","divisions":[{"label":"Title","span":{"begin":0,"end":14}}],"tracks":[]}