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Stereoelectronic and hydrogen-bonding effects on hydroxyproline conformation.

Fumiki Matsumura¹, Pablo Gómez Argudo^1,2, Mischa Bonn¹

¹Department of the Molecular Spectroscopy, Max Planck Institute for Polymer Research, Mainz, Germany.

Communications Chemistry

|March 25, 2026

Summary

The diastereomer (2S,4S)-4-hydroxyproline reduces collagen stability. Hydrogen bonding, not stereoelectronic effects, is key, with (2S,4S)-4-hydroxyproline favoring intramolecular bonds and (2S,4R)-4-hydroxyproline favoring intermolecular bonds.

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Area of Science:

Biochemistry
Structural Biology
Spectroscopy

Background:

Collagen's triple helix structure is crucial for its function and stability.
The amino acid (2S,4R)-hydroxyproline (4R-Hyp) is essential for collagen's triple helix.
Its diastereomer, (2S,4S)-4-hydroxyproline (4S-Hyp), significantly reduces thermal stability and impairs collagen function.

Purpose of the Study:

To investigate the molecular origins of destabilization caused by 4S-Hyp substitution in collagen.
To differentiate the roles of stereoelectronic effects and hydrogen bonding in hydroxyproline conformation.
To understand how different hydroxyproline isomers influence molecular conformation and interactions.

Main Methods:

Linear and two-dimensional infrared (2D IR) spectroscopy were used to study model compounds.
Density functional theory (DFT) calculations aided in analyzing molecular conformations.
The study focused on N-Boc-(2S,4S)-4-hydroxyproline-methyl ester (Boc-4S-Hyp-OMe) and N-Boc-(2S,4R)-4-hydroxyproline-methyl ester (Boc-4R-Hyp-OMe) in chloroform.

Main Results:

Stereoelectronic effects, including n → π* interactions, have a moderate impact on conformational equilibria.
Hydrogen bonding plays a pivotal role in determining hydroxyproline conformation.
Boc-4S-Hyp-OMe is stabilized by an intramolecular hydrogen bond, while Boc-4R-Hyp-OMe predominantly forms intermolecular hydrogen bonds, enhancing intermolecular affinity.

Conclusions:

Hydrogen bonding is the primary determinant of hydroxyproline conformation at the single-residue level.
The differing hydrogen bonding preferences of 4S-Hyp and 4R-Hyp explain the observed differences in collagen stability.
Understanding these interactions is crucial for comprehending collagen assembly and function.