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Programmed Assembly of Host-Guest Protein Crystals
Thaddaus R Huber1, Luke F Hartje1, Eli C McPherson1
1Chemical and Biological Engineering, Colorado State University, 1301 Campus Delivery, Fort Collins, Colorado, 80523, USA.
Small (Weinheim an Der Bergstrasse, Germany)
|December 8, 2016
Summary
Controlled binding and release of fluorescent proteins within protein crystals is achieved. This enables spatially segregated loading and the creation of hollow crystalline shells through selective exterior stabilization.
Area of Science:
- Biophysics
- Materials Science
- Nanotechnology
Background:
- Protein crystals offer unique nanostructures for controlled molecular interactions.
- Precise control over guest molecule loading and release within porous materials is challenging.
Purpose of the Study:
- To demonstrate controlled binding and release of guest fluorescent proteins within protein crystals.
- To achieve spatially segregated guest protein loading.
- To create hollow crystalline shells via selective crystal exterior stabilization.
Main Methods:
- Utilizing protein crystals with 13 nm axial pores.
- Implementing sequential binding and release stages for guest proteins.
- Applying selective stabilization techniques to the crystal exterior.
Main Results:
- Demonstrated controlled binding and release dynamics of guest fluorescent proteins.
- Achieved spatially segregated loading of different guest proteins.
- Successfully fabricated hollow crystalline shells with controlled porosity.
Conclusions:
- The study presents a method for precise control over guest molecule incorporation in protein crystals.
- This approach allows for the creation of functional nanomaterials with tailored internal structures.
- The developed technique has potential applications in drug delivery and biosensing.
