conformationally constrained peptides with remarkable properties
Krištof Bozovičar (Avtor), Tomaž Bratkovič (Avtor)

Povzetek

The sheer size and vast chemical space (i.e., diverse repertoire and spatial distribution of functional groups) underlie peptides' ability to engage in specific interactions with targets of various structures. However, the inherent flexibility of the peptide chain negatively affects binding affinity and metabolic stability, thereby severely limiting the use of peptides as medicines. Imposing conformational constraints to the peptide chain offers to solve these problems but typically requires laborious structure optimization. Alternatively, libraries of constrained peptides with randomized modules can be screened for specific functions. Here, we present the properties of conformationally constrained peptides and review rigidification chemistries/strategies, as well as synthetic and enzymatic methods of producing macrocyclic peptides. Furthermore, we discuss the in vitro molecular evolution methods for the development of constrained peptides with pre-defined functions. Finally, we briefly present applications of selected constrained peptides to illustrate their exceptional properties as drug candidates, molecular recognition probes, and minimalist catalysts.

Ključne besede

constrained peptides;macrocycles;crosslinking;enzymatic cyclization;stapling;hairpin loop;

Podatki

Jezik: Angleški jezik
Leto izida:
Tipologija: 1.02 - Pregledni znanstveni članek
Organizacija: UL FFA - Fakulteta za farmacijo
UDK: 543.645.6:615
COBISS: 50385155 Povezava se bo odprla v novem oknu
ISSN: 1422-0067
Št. ogledov: 167
Št. prenosov: 60
Ocena: 0 (0 glasov)
Metapodatki: JSON JSON-RDF JSON-LD TURTLE N-TRIPLES XML RDFA MICRODATA DC-XML DC-RDF RDF

Ostali podatki

Sekundarni jezik: Slovenski jezik
Sekundarne ključne besede: Peptidi;
Vrsta dela (COBISS): Članek v reviji
Strani: str. 1-25
Letnik: ǂVol. ǂ22
Zvezek: ǂiss. ǂ4
Čas izdaje: 2021
DOI: 10.3390/ijms22041611
ID: 14495768