Congeneric bio-adhesive mussel foot proteins designed by modified prolines revealed a chiral bias in unnatural translation

Larregola, Maud; Moore, Shannon; Budiša, Nediljko

doi:10.1016/j.bbrc.2012.04.031

Cited by 20 publications

(13 citation statements)

References 27 publications

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“…For example, selective pressure incorporation (SPI) has resulted in the global substitution of 4-fluoroproline for proline by conditioning bacterial protein synthesis through genetic engineering and the control of environmental factors such as amino acid supply and fermentation parameters [100–105]. Alternatively, the site-specific incorporation of 4-fluoroproline into proteins bearing multiple proline residues has been achieved by the chemical ligation of peptides possessing 4-fluoroproline residues to protein fragments produced by recombinant DNA technology [106].…”

Section: Effects On Protein Foldingmentioning

confidence: 99%

4-Fluoroprolines: Conformational Analysis and Effects on the Stability and Folding of Peptides and Proteins

Newberry

Raines

2016

Topics in Heterocyclic Chemistry

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Proline is unique among proteinogenic amino acids because a pyrrolidine ring links its amino group to its side chain. This heterocycle constrains the conformations of the main chain and thus templates particular secondary structures. Proline residues undergo post-translational modification at the 4-position to yield 4-hydroxyproline, which is especially prevalent in collagen. Interest in characterizing the effects of this modification led to the use of 4-fluoroprolines to enhance inductive properties relative to the hydroxyl group of 4-hydroxyproline and to eliminate contributions from hydrogen bonding. The strong inductive effect of the fluoro group has three main consequences: enforcing a particular pucker upon the pyrrolidine ring, biasing the conformation of the preceding peptide bond, and accelerating cis/trans prolyl peptide bond isomerization. These subtle, yet reliable modulations make 4-fluoroproline–incorporation a complement to traditional genetic approaches for exploring structure–function relationships in peptides and proteins, as well as for endowing peptides and proteins with conformational stability.

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Section: Effects On Protein Foldingmentioning

confidence: 99%

4-Fluoroprolines: Conformational Analysis and Effects on the Stability and Folding of Peptides and Proteins

Newberry

Raines

2016

Topics in Heterocyclic Chemistry

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“…The addition of non-natural amino acids has also extended the applicability of these materials, indicating that the transition temperatures, nanoparticulate morphology, and final thermal and mechanical properties can be precisely engineered. These techniques have been extended to biomaterials for applications such as bioadhesives [186], another important class of genetically encoded biomaterials that has benefited from the incorporation and investigation of non-canonical amino acids [187]. …”

Section: Discussion and Future Directionsmentioning

confidence: 99%

Designing protein-based biomaterials for medical applications

2014

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Biomaterials produced by nature have been honed through billions of years, evolving exquisitely precise structure-function relationships that scientists strive to emulate. Advances in genetic engineering have facilitated extensive investigations to determine how changes in even a single peptide within a protein sequence can produce biomaterials with unique thermal, mechanical and biological properties. Elastin, a naturally occurring protein polymer, serves as a model protein to determine the relationship between specific structural elements and desirable material characteristics. The modular, repetitive nature of the protein facilitates the formation of well-defined secondary structures with the ability to self-assemble into complex three-dimensional architectures on a variety of length scales. Furthermore, many opportunities exist to incorporate other protein-based motifs and inorganic materials into recombinant protein-based materials, extending the range and usefulness of these materials in potential biomedical applications. Elastin-like polypeptides can be assembled into 3D architectures with precise control over payload encapsulation, mechanical and thermal properties, as well as unique functionalization opportunities through both genetic and enzymatic means. An overview of current protein-based materials, their properties and uses in biomedicine will be provided, with a focus on the advantages of elastin-like polypeptides. Applications of these biomaterials as imaging and therapeutic delivery agents will be discussed. Finally, broader implications and future directions of these materials as diagnostic and therapeutic systems will be explored.

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“…16 At the same time, γ‐substitution of proline maintains the compatibility of the amino acid with the ribosomal machinery 15g,i,k,l,m,o. 17…”

Section: Methodsmentioning

confidence: 99%

Room‐Temperature Phosphorescence of Crystalline 1,4‐Bis(aroyl)‐2,5‐dibromobenzenes (Eur. J. Org. Chem. 3/2016)

2016

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The cover picture shows optical and phosphorescent images of 2,5‐dibromo‐1,4‐bis(4‐trifluoromethylphenylcarbonyl)benzene in crystals under ambient conditions with a simplified Jablonski diagram and the molecular structure of 1,4‐bis(aroyl)‐2,5‐dibromobenzene. The room‐temperature phosphorescence is observed only in crystals, but neither in solution nor in a doped polymer film. Thus, a class of the bis(aroyl)benzenes can serve as chromophores that exhibit crystallization‐induced room‐temperature phosphorescence. Intramolecular motion resulting in the energy loss in the triplet excited states is suppressed by several kinds of intermolecular interactions in crystals. Details are discussed in the article by M. Shimizu et al. on p. . The authors would like to warmly thank Ms. Kuniko Kayama for artistic inspiration and assistance in preparation of this cover picture.

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Congeneric bio-adhesive mussel foot proteins designed by modified prolines revealed a chiral bias in unnatural translation

Cited by 20 publications

References 27 publications

4-Fluoroprolines: Conformational Analysis and Effects on the Stability and Folding of Peptides and Proteins

4-Fluoroprolines: Conformational Analysis and Effects on the Stability and Folding of Peptides and Proteins

Designing protein-based biomaterials for medical applications

Room‐Temperature Phosphorescence of Crystalline 1,4‐Bis(aroyl)‐2,5‐dibromobenzenes (Eur. J. Org. Chem. 3/2016)

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