Molecular Structure of the Collagen Triple Helix

Brodsky, Barbara; Persikov, Anton V.

doi:10.1016/s0065-3233(05)70009-7

Cited by 505 publications

(491 citation statements)

References 111 publications

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“…Ac-Clp-OMe has a stronger preference for a trans amide bond than does Ac-ProOMe, whereas Ac-clp-OMe has a weaker preference. (Pro-Clp-Gly) 10 forms triple helices that are significantly more stable than those of (Pro-Pro-Gly) 10 . Triple helices of (clp-Pro-Gly) 10 have stability similar to those of (Pro-Pro-Gly) 10 .…”

Section: Introductionmentioning

confidence: 97%

4‐Chloroprolines: Synthesis, conformational analysis, and effect on the collagen triple helix

2007

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Collagen is an abundant, triple-helical protein comprising three strands of the repeating sequence: Xaa-Yaa-Gly. (2S)-Proline and (2S,4R)-4-hydroxyproline (Hyp) are common in the primary structure of collagen. Here, we use nonnatural proline derivatives to reveal determinants of collagen stability. Specifically, we report high-yielding syntheses of (2S,4S)-4-chloroproline (clp) and (2S, 4R)-4-chloroproline (Clp). We find that the crystal structure of Ac-Clp-OMe is virtually identical to that of Ac-Hyp-OMe. In contrast, the conformational properties of Ac-clp-OMe are similar to those of Ac-Pro-OMe. Ac-Clp-OMe has a stronger preference for a trans amide bond than does Ac-ProOMe, whereas Ac-clp-OMe has a weaker preference. (Pro-Clp-Gly) 10 forms triple helices that are significantly more stable than those of (Pro-Pro-Gly) 10 . Triple helices of (clp-Pro-Gly) 10 have stability similar to those of (Pro-Pro-Gly) 10 . Unlike (Pro-Clp-Gly) 10 and (clp-Pro-Gly) 10 , (clpClp-Gly) 10 does not form a stable triple helix, presumably due to a deleterious steric interaction between proximal chlorines on different strands. These data, which are consistent with previous work on 4-fluoroprolines and 4-methylprolines, support the importance of stereoelectronic and steric effects in the stability of the collagen triple helix and provide another means to modulate that stability.

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Section: Introductionmentioning

confidence: 97%

4‐Chloroprolines: Synthesis, conformational analysis, and effect on the collagen triple helix

2007

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“…In contrast, CPDY is characterized as an exopeptidase that typically cleaves only amide bonds at C-termini. Therefore, CPDY-catalyzed polymerization avoids the hydrolysis of the polypeptide backbones of pre-existing polypeptides, resulting in efficient suppression of the broadening of the molecular weight distribution of the products that Methyl, [49,54] ethyl, [50][51][52][53][54][55][56] benzyl [54] Proteinase I, [49] papain (13)(14)(15)(16)(17)(18) [50][51][52][53][54][55][56] Glycine Methyl, [54] ethyl, [49,51,54,55] benzyl [54] Proteinase I, [49] papain (10)(11)(12)(13)(14)(15)(16)(17)(18)(19) [51,54,55] l-Leucine…”

Section: Materials and General Protocolsmentioning

confidence: 99%

“…Ethyl, [49] isopropyl [23,24] Proteinase I, [49] papain (5)(6)(7)(8)(9)(10)(11)(12)(13)(14), [60,67,68] α-chymotrypsin [23,24] l-Lysine…”

Section: Materials and General Protocolsmentioning

confidence: 99%

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Chemoenzymatic Synthesis of Polypeptides for Use as Functional and Structural Materials

Tsuchiya

Numata

2017

Macromolecular Bioscience

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Polypeptides inspired by the natural functional and structural proteins present in living systems are promising materials for various fields in terms of their versatile functionality and physical properties. Designing and synthesizing mimetic sequences of specific peptide motifs in proteins are important for exploring the functionality of natural proteins. Chemoenzymatic polymerization, which utilizes aminolysis (i.e., the reverse reaction of hydrolysis catalyzed by proteases), is a useful technique for synthesizing artificial polypeptide materials and has several advantages, including facile synthesis protocols, environmental friendliness, scalability, and atom economy. In this review, recent progress in chemoenzymatic polypeptide synthesis for the production of functional and structural materials for various applications is summarized in conjunction with the current status of technical challenges in the field.

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“…X-ray fibre diffraction studies in the 1950s and recent X-ray crystallography of collagen-like peptides have provided information about the collagen triple helix at atomic resolution (for reviews, see [1,2]). However, most collagens function as part of supramolecular assemblies, which are refractory to study by conventional high-resolution techniques.…”

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confidence: 99%

Collagen pretzels revealed by electron microscopy

Kadler

2007

Biochemical Journal

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Collagen XV is a million-dalton protein with a structural role in skeletal muscle and capillaries. As with all collagens, studies of its function are hindered by the absence of good structural data: collagens are triple-helical, non-crystallizable, multidomain proteins with extensive post-translational modification that are refractory to analysis by high-resolution structural techniques. For collagen XV, this situation is compounded by the fact that it is also a proteoglycan. In this issue of the Biochemical Journal, Myers and her colleagues use rotary shadowing electron microscopy to obtain images of purified collagen XV molecules that are sufficiently detailed to show the three-lobed structure of the N-terminus and individual glycosaminoglycan side chains. Individual molecules appear as knotted strands resembling a pretzel (a pastry snack folded in a unique figure-of-eight), which contrasts with our conventional image of collagen molecules as semi-rigid rods. Importantly, collagen XV multimerizes into cruciform structures in which simpler forms have two to four molecules per complex. Immunoelectron microscopy revealed knotted collagen XV complexes bridging collagen fibrils adjacent to basement membrane. These accomplishments are made all the more impressive by the fact that collagen XV was purified from human umbilical cord, in which the protein is represented at only (1−2) × 10 −4 % of dry weight! Key words: basement membrane, collagen, electron tomography, endostatin, extracellular matrix, fibril, rotary shadowing.Understanding the structure and assembly of collagens has occupied the attention of matrix biologists and structural biologists for many years. X-ray fibre diffraction studies in the 1950s and recent X-ray crystallography of collagen-like peptides have provided information about the collagen triple helix at atomic resolution (for reviews, see [1,2]). However, most collagens function as part of supramolecular assemblies, which are refractory to study by conventional high-resolution techniques. Consequently, important questions about the structure of native collagens and how they assemble in vivo remain unanswered.Studies in the 1960s-1980s used electron microscopy to record detailed images of type I collagen (the major collagen, found in skin and tendon) and the 67 nm D-periodic fibrils that are formed by self-assembly of type I collagen molecules (for a review, see [3]). In subsequent years other collagens were identified that assemble into extended networks (e.g. collagens IV, VIII and X), anchoring filaments (collagen VII), beaded narrowdiameter microfibrils (e.g. collagen VI), and FACIT (fibril-associated collagens with interrupted triple helices) collagens that bind to the surfaces of collagen fibrils and provide binding sites for ECM (extracellular matrix) macromolecules (for a review, see [4]). We could be forgiven for thinking that we had seen the complete array of supramolecular assembles that collagen could form. Then along came the paper by Myers and colleagues in this issue of the Bioche...

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Molecular Structure of the Collagen Triple Helix

Cited by 505 publications

References 111 publications

4‐Chloroprolines: Synthesis, conformational analysis, and effect on the collagen triple helix

4‐Chloroprolines: Synthesis, conformational analysis, and effect on the collagen triple helix

Chemoenzymatic Synthesis of Polypeptides for Use as Functional and Structural Materials

Collagen pretzels revealed by electron microscopy

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