Articolo in rivista, 2018, ENG, 10.1080/10409238.2018.1447543
Iavarone F.; Desiderio C.; Vitali A.; Messana I.; Martelli C.; Castagnola M.; Cabras T.
Istituto di Biochimica e Biochimica Clinica, Università Cattolica, Roma, , Italy; Istituto di Chimica del Riconoscimento Molecolare, CNR, Roma, , Italy; Dipartimento di Scienze della Vita e dell'Ambiente, Università di Cagliari, Cagliari, , Italy
Proteomic surveys with top-down platforms are today revealing thousands of naturally occurring fragments of bigger proteins. Some of them have not functional meaning because they derive from pathways responsible for protein degradation, but many have specific functions, often completely different from that one of the parent proteins. These peptides encrypted in the protein sequence are nowadays called cryptides. They are frequent in the animal and plant kingdoms and represent a new interesting -omic field of investigation. To point out how much widespread is their presence, we describe here the most studied cryptides from very common sources such as serum albumin, immunoglobulins, hemoglobin, and from saliva and milk proteins. Given its vastness, it is unfeasible to cover the topic exhaustively, therefore only several selected examples of cryptides from other sources are thereafter reported. Demanding is the development of new -omic platforms for the functional screening of new cryptides, which could provide suggestion for peptides and peptido-mimetics with variegate fields of application.
Critical reviews in biochemistry and molecular biology (Online) 53 (3), pp. 246–263
albumin, Cryptides, encrypted peptides, hemoglobin, hemorphins, hidden peptides, immunoglobulins, latent peptides
Castagnola Massimo, Messana Irene, Desiderio Claudia, Vitali Alberto
ID: 388439
Year: 2018
Type: Articolo in rivista
Creation: 2018-06-20 10:20:21.000
Last update: 2022-06-07 12:32:56.000
CNR institutes
External links
OAI-PMH: Dublin Core
OAI-PMH: Mods
OAI-PMH: RDF
DOI: 10.1080/10409238.2018.1447543
URL: http://www.scopus.com/inward/record.url?eid=2-s2.0-85046548578&partnerID=q2rCbXpz
External IDs
CNR OAI-PMH: oai:it.cnr:prodotti:388439
DOI: 10.1080/10409238.2018.1447543
Scopus: 2-s2.0-85046548578
ISI Web of Science (WOS): 000431534600002