Self-Assembly of Collagen Triple Helices into Higher Order Structures

NSF Award Search · 01002526DB NSF RESEARCH & RELATED ACTIVIT · $600,000 · view on nsf.gov ↗

Abstract

With the support of the Macromolecular, Supramolecular, and Nanochemistry Program in the Division of Chemistry, Dr. Jeffrey D. Hartgerink of Rice University aims to reveal the atomic structure of collagen, the most abundant protein in the human body. Collagen is a remarkable protein which undergoes multiple levels of assembly. The beautiful final product controls an incredibly wide range of biological behavior including tissue integrity, cancer metastasis, wound healing, effective response to viral and bacterial invaders, and even weight regulation. Amazingly, despite early studies dating back to the 1950’s, collagen is very poorly understood. Without an accurate structure, advances in all these areas will be limited. The research team has recently discovered that bundled collagen can take on a never-before-observed shape. The team will explore the circumstances under which this novel shape is formed, undertaking studies with potential to reveal the mysteries of collagen superstructure that have evaded sight for over seventy years. This work expects to lay out chemical methods allowing scientists to mimic biological materials, which may lead to breakthroughs in tissue regeneration, immunology, and cancer research. This program will also serve as the basis to train the next generation of scientists including graduate students pursuing a PhD, undergraduates pursuing Chemistry and Bioscience degrees, and enhancing the pipeline of STEM focused students by engaging high school stu

Key facts

NSF award ID
2505948
Awardee
William Marsh Rice University (TX)
SAM.gov UEI
K51LECU1G8N3
PI
Jeffrey D Hartgerink
Primary program
01002526DB NSF RESEARCH & RELATED ACTIVIT
All programs
RET SUPP-Res Exp for Tchr Supp
Estimated total
$600,000
Funds obligated
$600,000
Transaction type
Standard Grant
Period
07/01/2025 → 06/30/2028