# STRUCTURE AND ASSEMBLY OF COLLAGEN MOLECULES AND FIBRILS

> **NIH NIH R01** · NORTHWESTERN UNIVERSITY · 1987 · $189,552

## Abstract

Collagen molecules are the principal structural elements of all connective
tissues.  Collagen fiber organization and ultrastructure varies from one
tissue to the next.  The objective of this study is to delineate the basic
molecular events which are involved in the molecular fibril assembly
processes and to determine the factors which regulate these processes.
Four specific aspects of assembly are to be examined in detail.  1) Nascent
pro Alpha chains register in the appropriate stoichiometry and initiate
triple helix formation as the chains near release from the endoplasmic
reticulum membrane.  Membrane mediated interactions may guide this phase of
assembly.  A combination of cell-free translation, polysome isolation and
completion, and membrane insertion studies will be used to examine the
chain assembly mechanism.  2) Interstitial procollagens must be processed
at both COOH - and NH2-propeptides before stable fibrils form.  The
NH2-propeptidase activity is well understood whereas the COOH- propeptidase
has not been isolated and the site of its action not determined.  Evidence
is accumulating that the COOH-propeptide cleavage might be tied in with
late stages of intracellular secretory processing and regulation of
intracellular degradation.  The processing localization of this event, and
its enzymology are to be examined in detail.  3) Fibril formation is an
event dominated by telopeptide-helix receptor region interactions.  The
explicit chemistry of this interaction, and the properties of these
molecular domains are to be examined by interaction studies between
isolated peptides, by physical studies (CD, FT-IR), and by interaction and
conformational predictive studies.  4) Type IV basement membrane collagens
form filamentous networks rather than fibrils, from molecules which are
minimally processed and retain extensive non-triplet sequence chain
segments.  Anterior lens-capsule Type IV collagen can be obtained with
minimal degradation.  The self-assembly process will be examined, by
thermal self-assembly studies and various electron microscopic techniques
including SLS formation and rotary shadowing.  From all these studies we
should develop better insights into the synthesis and construction of the
collagenous framework of the connective tissues.  Our studies of the
mechanism of molecular assembly and tissue ordering have the ultimate
objective of providing insight into the control of the connective tissue
disorders and their treatment.

## Key facts

- **NIH application ID:** 3154794
- **Project number:** 5R01AR013921-27
- **Recipient organization:** NORTHWESTERN UNIVERSITY
- **SAM.gov UEI:** KG76WYENL5K1
- **Principal Investigator:** ARTHUR VEIS
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1987
- **Award amount:** $189,552
- **Award type:** 5
- **Project period:** 1979-03-01 → 1989-02-28

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3154794

## Citation

> US National Institutes of Health, RePORTER application 3154794, STRUCTURE AND ASSEMBLY OF COLLAGEN MOLECULES AND FIBRILS (5R01AR013921-27). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3154794. Licensed CC0.

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