This paper reveals the mechanism of nanowelding a branched network of single-walled carbon nanotubes (SWCNTs) used as a framework for the formation of protein-polymer matrices with albumin, collagen, and chitosan. It is shown that the introduction of certain point defects into the structure of SWCNTs (single vacancy, double vacancy, Stone-Wales defect, and a mixed defect) allows us to obtain strong heating in defective regions as compared to ideal SWCNTs. The wavelengths at which absorption reaches 50% are determined. Non-uniform absorption of laser radiation along with inefficient heat removal in defective regions determines the formation of hot spots, in which nanowelding of SWCNTs is observed even at 0.36 nm between contacting surfaces. The regularities of formation of layered protein-polymer matrices and the features of their interaction with cell membrane are revealed. All studies are carried out in silico using high-precision quantum approaches.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6803951PMC
http://dx.doi.org/10.3390/ma12193083DOI Listing

Publication Analysis

Top Keywords

protein-polymer matrices
12
carbon nanotubes
8
regularities formation
8
features interaction
8
interaction cell
8
defective regions
8
matrices embedded
4
embedded carbon
4
nanotubes tissue
4
tissue engineering
4

Similar Publications

Hot-melt extrusion (HME) is used for the production of solid protein formulations mainly for two reasons: increased protein stability in solid state and/or long-term release systems (e.g., protein-loaded implants).

View Article and Find Full Text PDF

Field-flow fractionation for molecular-interaction studies of labile and complex systems: A critical review.

Anal Chim Acta

February 2022

University of Amsterdam, van 't Hoff Institute for Molecular Sciences, Analytical-Chemistry Group, Science Park 904, 1098 XH Amsterdam, the Netherlands; Centre of Analytical Sciences Amsterdam, Science Park, 904, 1098 XH Amsterdam, the Netherlands.

Asymmetrical flow field-flow fractionation (AF4) has attracted considerable attention as a size-based separation technique, due to its mild separation conditions, broad working range (from approximately 10 to 10 Da molecular mass or from 1 nm to 1 μm particle diameter), and versatility. AF4 is primarily being used to measure particle size, polydispersity, and physical stability of various systems, such as (bio)-macromolecules and nanoparticles. In comparison with size-exclusion chromatography (packed column), AF4 (open channel) allows separation while preserving labile structures.

View Article and Find Full Text PDF

Differences in Mixolab measurements of dough processing were examined using, as a base, flour from pure breeding, isogenic, wheat lines carrying either the high molecular weight glutenin subunits 5 + 10 or 2 + 12. Before dough pasting, subunits 5 + 10 tend to form a stable gluten network relying mainly on disulfide bonds and hydrogen bonds, but 2 + 12 flour was prone to generating fragile protein aggregates dominated by disulfide bonds and hydrophobicity. During dough pasting, a broader protein network rich in un-extractable polymeric proteins, disulfide bonds and β-sheets was formed in the dough with subunits 5 + 10, thus resulting in an extensive and compact protein-starch complex which was characterized by high thermal stability and low starch gelatinization, while in the dough of the 2 + 12 line, a porous protein-starch gel with fragmented protein aggregates was controlled by the combination of disulfide bonds, hydrophobicity and hydrogen bonds that facilitated the formation of antiparallel β-sheets.

View Article and Find Full Text PDF

Many current strategies for inducing an immune response rely on the production of an antigenic protein. Such methods can be problematic if the folding of the antigenic protein is incorrect. To avoid this problem, we propose a method based on grafting specific regions of the chosen antigenic protein onto biocompatible polymeric matrices, so that they can mimic portions of the antigenic protein.

View Article and Find Full Text PDF

Many extracellular matrices (ECM) used for modern cell culture are derived from animals. An alternative approach is the recombinant production of individual matrix protein components. A further development of this strategy uses a constant core protein polymer that is modifiable with functional domains of various ECM proteins.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!