RT info:eu-repo/semantics/article
T1 Self‐assembling systems comprising intrinsically disordered protein polymers like elastin‐like recombinamers
A1 Juanes Gusano, Diana
A1 Santos García, María Mercedes
A1 Reboto Rodríguez, Virginia
A1 Alonso Rodrigo, Matilde
A1 Rodríguez Cabello, José Carlos
K1 Biomineralization
K1 Elastin
K1 Elastin-like recombinamers
K1 Self-assembling
K1 22 Física
K1 23 Química
K1 24 Ciencias de la Vida
AB Despite lacking cooperatively folded structures under native conditions, numerous intrinsically disordered proteins (IDPs) nevertheless have great functional importance. These IDPs are hybrids containing both ordered and intrinsically disordered protein regions (IDPRs), the structure of which is highly flexible in this unfolded state. The conformational flexibility of these disordered systems favors transitions between disordered and ordered states triggered by intrinsic and extrinsic factors, folding into different dynamic molecular assemblies to enable proper protein functions. Indeed, prokaryotic enzymes present less disorder than eukaryotic enzymes, thus showing that this disorder is related to functional and structural complexity. Protein-based polymers that mimic these IDPs include the so-called elastin-like polypeptides (ELPs), which are inspired by the composition of natural elastin. Elastin-like recombinamers (ELRs) are ELPs produced using recombinant techniques and which can therefore be tailored for a specific application. One of the most widely used and studied characteristic structures in this field is the pentapeptide (VPGXG)n. The structural disorder in ELRs probably arises due to the high content of proline and glycine in the ELR backbone, because both these amino acids help to keep the polypeptide structure of elastomers disordered and hydrated. Moreover, the recombinant nature of these systems means that different sequences can be designed, including bioactive domains, to obtain specific structures for each application. Some of these structures, along with their applications as IDPs that self-assemble into functional vesicles or micelles from diblock copolymer ELRs, will be studied in the following sections. The incorporation of additional order- and disorder-promoting peptide/protein domains, such as α-helical coils or β-strands, in the ELR sequence, and their influence on self-assembly, will also be reviewed. In addition, chemically cross-linked systems with controllable order–disorder balance, and their role in biomineralization, will be discussed. Finally, we will review different multivalent IDPs-based coatings and films for different biomedical applications, such as spatially controlled cell adhesion, osseointegration, or biomaterial-associated infection (BAI).
PB Wiley
SN 1075-2617
YR 2021
FD 2021
LK https://uvadoc.uva.es/handle/10324/53958
UL https://uvadoc.uva.es/handle/10324/53958
LA eng
NO Journal of Peptide Science, 2021, vol. 28, n. 1 e.3362
NO Producción Científica
DS UVaDOC
RD 04-dic-2024