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Updated: Feb 8, 2026
09:42
Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides
Published on: June 19, 2012
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Tuning the Stiffness of Surfaces by Assembling Genetically Engineered Polypeptides with Tailored Amino Acid Sequence
Rui R Costa1,2, Miguel González-Pérez3,4, Marcos Herrero-Gutiérrez3,4
13B's Research Group, I3Bs-Research Institute on Biomaterials, Biodegradables and Biomimetics , University of Minho, Headquarters of the European Institute of Excellence on Tissue Engineering and Regenerative Medicine , AvePark, Parque de Ciência e Tecnologia, Zona Industrial da Gandra , 4805-017 Barco, Guimarães , Portugal.
Biomacromolecules
|July 4, 2018
Summary
We developed tunable polypeptide coatings using elastin-like recombinamers (ELRs). Their adsorption behavior and layer properties depend on amino acid sequence and surface chemistry, influencing coating stiffness.
Area of Science:
- Biomaterials Science
- Polymer Chemistry
- Surface Science
Background:
- Elastin-like recombinamers (ELRs) are polypeptides with programmable sequences.
- Controlling polypeptide coating properties like rigidity is crucial for biomaterial applications.
- Understanding ELR-surface interactions is key to designing advanced materials.
Purpose of the Study:
- To introduce ELRs as a platform for creating polypeptide coatings with tunable rigidity.
- To investigate the influence of ELR amino acid sequence and surface chemistry on adsorption and layer properties.
- To characterize the conformation and dissipative behavior of ELR coatings.
Main Methods:
- Synthesis and modification of two distinct ELRs (V84-ELR and EI-ELR).
- Assembly of ELR coatings on alkanethiol self-assembled monolayers.
- Characterization using quartz crystal microbalance with dissipation monitoring (QCM-D), multiparametric surface plasmon resonance (MP-SPR), and atomic force microscopy (AFM).
Main Results:
- ELRs exhibited preferential affinity to NH2- and CH3-terminated surfaces.
- V84-ELR formed strongly bonded, extended, and hydrated layers with increasing adsorption.
- EI-ELR displayed less dissipative behavior compared to V84-ELR.
- Adsorption behavior and layer properties were influenced by ELR sequence and substrate chemistry.
Conclusions:
- ELRs provide a versatile tool for engineering polypeptide coatings with tunable mechanical properties.
- The interplay between ELR amino acid sequence and surface chemistry dictates coating characteristics.
- This work offers insights into designing biomaterials with tailored stiffness and interfacial properties.
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