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Effect of sequence pattern on conformation of DOPA-Peptide conjugate aggregates: a discontinuous molecular dynamics simulation study.
- Source :
-
Molecular Simulation . 2023, Vol. 49 Issue 15, p1452-1464. 13p. - Publication Year :
- 2023
-
Abstract
- Underwater adhesives are critical for many applications, including marine coatings, sealants, and medical devices. Research on natural underwater adhesives has shown that L-3,4-dihydroxyphenylalanine (DOPA) and amyloid nanostructures are vital to their adhesive abilities. The fusion of DOPA-containing chains and amyloid-forming peptides creates a new space for designing underwater adhesives capable of multi-surface adhesion. One critical question for this design is the interplay between the DOPA and amyloid-forming peptide regions. Here we investigate the effect of the sequence pattern of DOPA-containing chains on the aggregation conformation of conjugates. Discontinuous molecular dynamics simulations were performed for fourteen DOPA-amyloid conjugates with different sequence patterns along the DOPA-containing portion. The amyloid-forming portion is represented by KLVFFAE from the Aβ42 peptide. The structural properties of the DOPA-amyloid conjugates are characterised by the percentages of ordered secondary structures and residue-residue contact maps. The results showed that certain patterns of DOPA and glycine in the DOPA-containing tail allowed the KLVFFAE portions of the conjugates to form distinct ordered β-sheets, and the DOPA-containing portion and the KLVFFAE portion of the conjugates to remain separated both within the same chain and amongst different chains. Among the designs, the most promising sequences are KLVFFAE-G-YYGYYGYY (where Y represents DOPA) and KLVFFAE-G-YYYYGGGG. [ABSTRACT FROM AUTHOR]
- Subjects :
- *MOLECULAR dynamics
*PEPTIDES
*AMYLOID
*DOPA
Subjects
Details
- Language :
- English
- ISSN :
- 08927022
- Volume :
- 49
- Issue :
- 15
- Database :
- Academic Search Index
- Journal :
- Molecular Simulation
- Publication Type :
- Academic Journal
- Accession number :
- 171310506
- Full Text :
- https://doi.org/10.1080/08927022.2023.2240911