Next Article in Journal
“Skin-Core-Skin” Structure of Polymer Crystallization Investigated by Multiscale Simulation
Previous Article in Journal
Microstructure and Mechanical Properties of Graphene-Reinforced Titanium Matrix/Nano-Hydroxyapatite Nanocomposites
Article Menu
Issue 4 (April) cover image

Export Article

Open AccessArticle
Materials 2018, 11(4), 609; doi:10.3390/ma11040609

Customized Peptide Biomaterial Synthesis via an Environment-Reliant Auto-Programmer Stigmergic Approach

1
Wits Advanced Drug Delivery Platform Research Unit, Department of Pharmacy and Pharmacology, School of Therapeutic Sciences, Faculty of Health Sciences, University of the Witwatersrand, Johannesburg, 7 York Road, Parktown 2193, South Africa
2
Department of Refractories, Ceramics and Building Materials, National Research Centre, 33 El-Bohouth St. (former El-Tahrir St.), Dokki, Giza P.O. 12622, Egypt
*
Author to whom correspondence should be addressed.
Received: 1 March 2018 / Revised: 11 April 2018 / Accepted: 11 April 2018 / Published: 16 April 2018
(This article belongs to the Special Issue Advanced Nanomaterials and Biomaterials from Self-Assembling Peptides)
View Full-Text   |   Download PDF [25579 KB, uploaded 16 April 2018]   |  

Abstract

Stigmergy, a form of self-organization, was employed here to engineer a self-organizing peptide capable of forming a nano- or micro-structure and that can potentially be used in various drug delivery and biomedical applications. These self-assembling peptides exhibit several desirable qualities for drug delivery, tissue engineering, cosmetics, antibiotics, food science, and biomedical surface engineering. In this study, peptide biomaterial synthesis was carried out using an environment-reliant auto-programmer stigmergic approach. A model protein, α-gliadin (31, 36, and 38 kD), was forced to attain a primary structure with free –SH groups and broken down enzymatically into smaller fragments using chymotrypsin. This breakdown was carried out at different environment conditions (37 and 50 °C), and the fragments were allowed to self-organize at these temperatures. The new peptides so formed diverged according to the environmental conditions. Interestingly, two peptides (with molecular weights of 13.8 and 11.8 kD) were isolated when the reaction temperature was maintained at 50 °C, while four peptides with molecular weights of 54, 51, 13.8, and 12.8 kD were obtained when the reaction was conducted at 37 °C. Thus, at a higher temperature (50 °C), the peptides formed, compared to the original protein, had lower molecular weights, whereas, at a lower temperature (37 °C), two peptides had higher molecular weights and two had lower molecular weights. View Full-Text
Keywords: stigmergy; peptide biomaterial synthesis; self-organizing peptides; effect of temperature on protein digestion stigmergy; peptide biomaterial synthesis; self-organizing peptides; effect of temperature on protein digestion
Figures

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary material

Share & Cite This Article

MDPI and ACS Style

Badhe, R.V.; Kumar, P.; Choonara, Y.E.; Marimuthu, T.; du Toit, L.C.; Bijukumar, D.; Chejara, D.R.; Mabrouk, M.; Pillay, V. Customized Peptide Biomaterial Synthesis via an Environment-Reliant Auto-Programmer Stigmergic Approach. Materials 2018, 11, 609.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Materials EISSN 1996-1944 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top