This report describes the efficient conjugation of doxorubicin-glycine-phenylalanine-leucine-glycine (1a) and rhodamine-glycine-phenylalanine-leucine-glycine (1b) units to a monodisperse elastin-mimetic polypeptide (EMM)(7) bearing eight primary amine groups for chemical attachment. The synthetic approach is based on the solid-phase synthesis of 1a and 1b followed by chemical conjugation to the elastin-mimetic polypeptide in the presence of HOBt/PyBob as activating agents to form the polypeptide conjugates 2a and 2b. Conjugation efficiency was 61.2% (4.9 doxorubicin units per polypeptide chain) for 2a and 53.7% (4.3 rhodamine units per polypeptide chain) for 2b, demonstrating the feasibility of using these tailor-made, recombinant polypeptides as potential drug carriers for cancer therapy.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1002/mabi.200600117 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Bilayer Hydrogel Composed of Elastin-Mimetic Polypeptides as a Bio-Actuator with Bidirectional and Reversible Bending Behaviors.
Molecules
July 2023
Laboratory of Biological Chemistry, Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo 060-0810, Japan.
Biologically derived hydrogels have attracted attention as promising polymers for use in biomedical applications because of their high biocompatibility, biodegradability, and low toxicity. Elastin-mimetic polypeptides (EMPs), which contain a repeated amino acid sequence derived from the hydrophobic domain of tropoelastin, exhibit reversible phase transition behavior, and thus, represent an interesting starting point for the development of biologically derived hydrogels. In this study, we succeeded in developing functional EMP-conjugated hydrogels that displayed temperature-responsive swelling/shrinking properties.
View Article and Find Full Text PDFElastin-inspired supramolecular hydrogels: a multifaceted extracellular matrix protein in biomedical engineering.
Soft Matter
March 2021
Institute of Nano Science and Technology (INST), Sector 81, Knowledge City, Mohali, 140306, Punjab, India.
The phenomenal advancement in regenerative medicines has led to the development of bioinspired materials to fabricate a biomimetic artificial extracellular matrix (ECM) to support cellular survival, proliferation, and differentiation. Researchers have diligently developed protein polymers consisting of functional sequences of amino acids evolved in nature. Nowadays, certain repetitive bioinspired polymers are treated as an alternative to synthetic polymers due to their unique properties like biodegradability, easy scale-up, biocompatibility, and non-covalent molecular associations which imparts tunable supramolecular architecture to these materials.
View Article and Find Full Text PDFConstruction of multifunctional fusion proteins with a laminin-derived short peptide to promote neural differentiation of mouse induced pluripotent stem cells.
J Biomed Mater Res B Appl Biomater
August 2020
Department of Life Science and Technology, School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
There is growing interest in the functional roles of the extracellular matrix (ECM) in regulating the fate of pluripotent stem cells (PSCs). An artificially bioengineered ECM provides an excellent model for studying the molecular mechanisms underlying self-renewal and differentiation of PSCs, without multiple unknown and variable factors associated with natural substrates. Here, we have engineered multifunctional fusion proteins that are based on peptides from laminin, including p20, RGD, and elastin-like polypeptide (ELP), where laminin peptides work as cell adhesion molecules (CAMs) and ELP to promote anchorage.
View Article and Find Full Text PDFHydrophobic Cholesteryl Moieties Trigger Substrate Cell-Membrane Interaction of Elastin-Mimetic Protein Coatings in Vitro.
ACS Omega
June 2019
Bioforge, University of Valladolid CIBER-BNN, Paseo de Belén 19, 47011 Valladolid, Spain.
A cellular coating based on hydrophobic interactions of an elastin-like recombinamer (ELR) with the cell membrane is presented. It is well-documented that biophysical properties such as net charge, hydrophobicity, and protein-driven cell-ligand (integrin binding) interactions influence the interaction of polymers, proteins or peptides with model membranes and biological cells. Most studies to enhance membrane-substrate interactions have focused on the introduction of positively charged groups to foster electrostatic interactions with the negatively charged membrane.
View Article and Find Full Text PDFDouble-hydrophobic elastin-like polypeptides with added functional motifs: Self-assembly and cytocompatibility.
J Biomed Mater Res A
September 2017
Department of Crystalline Materials Science, Graduate School of Engineering, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, 464-8603, Japan.
We have recently developed a novel double-hydrophobic elastin-like triblock polypeptide called GPG, designed after the uneven distribution of two different hydrophobic domains found in elastin, an extracellular matrix protein providing elasticity and resilience to tissues. Upon temperature trigger, GPG undergoes a sequential self-assembling process to form flexible beaded nanofibers with high homogeneity and excellent dispersibility in water. Given that GPG might be a potential elastin-mimetic material, we sought to explore the biological activities of this block polypeptide.
View Article and Find Full Text PDFWant 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!