title: Structure and Function of AApeptides.
abstract: The intrinsic drawbacks encountered in bioactive peptides in chemical biology and biomedical sciences have diverted research efforts to the development of sequence-specific peptidomimetics that are capable of mimicking the structure and function of peptides and proteins. Modifications in the backbone and/or the side chain of peptides have been explored to develop biomimetic molecular probes or drug leads for biologically important targets. To expand the family of oligomeric peptidomimetics to facilitate their further application, we recently developed a new class of peptidomimetics, AApeptides based on a chiral peptide nucleic acid backbone. AApeptides are resistant to proteolytic degradation and amenable to enormous chemical diversification. Moreover, they could mimic the primary structure of peptides and also fold into discrete secondary structure such as helices and turn-like structures. Furthermore, they have started to show promise in applications in material and biomedical sciences. Herein, we highlight the structural design and some function of AApeptides and present our perspective on their future development.
authors.affiliation: Department of Chemistry, University of South Florida , 4202 East Fowler Avenue, Tampa, Florida 33620, United States.
authors.forename: Olapeju
authors.initials: O
authors.lastname: Bolarinwa
authors.affiliation: Department of Chemistry, University of South Florida , 4202 East Fowler Avenue, Tampa, Florida 33620, United States.
authors.forename: Alekhya
authors.initials: A
authors.lastname: Nimmagadda
authors.affiliation: Department of Chemistry, University of South Florida , 4202 East Fowler Avenue, Tampa, Florida 33620, United States.
authors.forename: Ma
authors.initials: M
authors.lastname: Su
authors.affiliation: Department of Chemistry, University of South Florida , 4202 East Fowler Avenue, Tampa, Florida 33620, United States.
authors.forename: Jianfeng
authors.identifier: http://orcid.org/0000-0003-3106-3306
authors.initials: J
authors.lastname: Cai
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D000890:Anti-Infective Agents / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D001593:Benzyl Compounds / Q000737:chemistry; D002176:Candida albicans / Q000187:drug effects / Q000254:growth & development; D003500:Cyclization; D005449:Fluorenes / Q000737:chemistry; D006090:Gram-Negative Bacteria / Q000187:drug effects / Q000254:growth & development; D006094:Gram-Positive Bacteria / Q000187:drug effects / Q000254:growth & development; D008826:Microbial Sensitivity Tests; D020135:Peptide Nucleic Acids / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D057786:Peptidomimetics / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D055550:Protein Stability; D017433:Protein Structure, Secondary; D059748:Proteolysis; D060327:Solid-Phase Synthesis Techniques; D013237:Stereoisomerism; D013329:Structure-Activity Relationship
chemical_list: D000596:Amino Acids; D000890:Anti-Infective Agents; D001593:Benzyl Compounds; D005449:Fluorenes; D020135:Peptide Nucleic Acids; D057786:Peptidomimetics