The Preparation of Enantiopure [6]- and [7]Helicenes from Binaphthanol

Key Words:DECREASED EXPRESSION; ZWITTERIONIC PEPTIDE; IN-VITRO; PROGRESSION; DELIVERY; VIVO

Abstract:Specific peptide-protein interactions play animportantrole in biosensing systems based on functional peptides; however,the non-specific interactions with unrelated biomolecules and poorproteolytic stability restrict the clinical application of naturalpeptides. Here, we leveraged a self-designed multifunctional isopeptide(MISP) to construct an electrochemical biosensing platform for annexinA1 (ANXA1) detection in human blood. The MISP was designed to containtwo parts: an antifouling cyclotide cyclo-C-(EK)(4) and a d-amino acid-containing carbohydrate-mimetic recognizing peptideIF-7 (D-IF7) connected by the isopeptide bond. We have discussed theproperties of the cyclotide and illustrated its unique advantage overthe natural linear antifouling peptides by molecular dynamics simulations,and the results were further confirmed by dissipative quartz crystalmicrobalance (QCM-D). In addition, through electrochemical experimentsand fluorescence imaging experiments, we demonstrated that the MISP-basedbiosensor possessed excellent antifouling ability and proteinase hydrolysisstability. Interestingly, the assaying results of the MISP-biosensorwere consistent with those of the commercial ANXA1 kits in a varietyof healthy and ANXA1-upregulated clinical blood samples, and, moreimportantly, for the analysis of blood samples with lower ANXA1 expressions,the sensing capability of the biosensor was greatly superior to thatof the kits because of the lower detection limit of the MISP-biosensor.This biosensing platform based on the designed MISP offers enormouspotential for achieving accurate biomarker detection with robust operationin complex biological samples.

Volume:95

Issue:23

Translation or Not:no