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  1. Article ; Online: Correction to "Incorporation of Aza-Glycine into Collagen Peptides".

    Melton, Samuel D / Smith, Mason S / Chenoweth, David M

    The Journal of organic chemistry

    2020  Volume 85, Issue 6, Page(s) 4582

    Language English
    Publishing date 2020-03-09
    Publishing country United States
    Document type Published Erratum
    ZDB-ID 123490-0
    ISSN 1520-6904 ; 0022-3263
    ISSN (online) 1520-6904
    ISSN 0022-3263
    DOI 10.1021/acs.joc.0c00497
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4473: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  2. Article ; Online: Incorporation of Aza-Glycine into Collagen Peptides.

    Melton, Samuel D / Smith, Mason S / Chenoweth, David M

    The Journal of organic chemistry

    2019  Volume 85, Issue 3, Page(s) 1706–1711

    Abstract: Substitution of natural amino acids with their aza-amino acid counterparts in peptides has been a historically challenging prospect due to the diminished reactivity of the involved reagents. Current methods require lengthy reaction times or difficult ... ...

    Abstract Substitution of natural amino acids with their aza-amino acid counterparts in peptides has been a historically challenging prospect due to the diminished reactivity of the involved reagents. Current methods require lengthy reaction times or difficult synthetic strategies. Aza-glycine has proven to be a valuable tool in the design of triple-helix-forming collagen peptides. Herein, we describe a method for incorporation of aza-glycine in collagen peptides, and we apply the method to the synthesis of collagen peptides containing multiple aza-glycine residues.
    MeSH term(s) Amino Acids ; Collagen ; Glycine ; Peptides
    Chemical Substances Amino Acids ; Peptides ; Collagen (9007-34-5) ; Glycine (TE7660XO1C)
    Language English
    Publishing date 2019-12-16
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 123490-0
    ISSN 1520-6904 ; 0022-3263
    ISSN (online) 1520-6904
    ISSN 0022-3263
    DOI 10.1021/acs.joc.9b02539
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4473: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  3. Article: Incorporation of Aza-Glycine into Collagen Peptides

    Melton, Samuel D / Smith, Mason S / Chenoweth, David M

    Journal of organic chemistry. 2019 Nov. 14, v. 85, no. 3

    2019  

    Abstract: Substitution of natural amino acids with their aza-amino acid counterparts in peptides has been a historically challenging prospect due to the diminished reactivity of the involved reagents. Current methods require lengthy reaction times or difficult ... ...

    Abstract Substitution of natural amino acids with their aza-amino acid counterparts in peptides has been a historically challenging prospect due to the diminished reactivity of the involved reagents. Current methods require lengthy reaction times or difficult synthetic strategies. Aza-glycine has proven to be a valuable tool in the design of triple-helix-forming collagen peptides. Herein, we describe a method for incorporation of aza-glycine in collagen peptides, and we apply the method to the synthesis of collagen peptides containing multiple aza-glycine residues.
    Keywords amino acids ; chemical reactions ; chemical structure ; collagen ; organic chemistry ; organic compounds ; peptides
    Language English
    Dates of publication 2019-1114
    Size p. 1706-1711.
    Publishing place American Chemical Society
    Document type Article
    ZDB-ID 123490-0
    ISSN 1520-6904 ; 0022-3263
    ISSN (online) 1520-6904
    ISSN 0022-3263
    DOI 10.1021/acs.joc.9b02539
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 4' 49/42: Show issues
    Z 7.1: Show issues

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  4. Article ; Online: Context-Dependent Stabilizing Interactions among Solvent-Exposed Residues along the Surface of a Trimeric Helix Bundle.

    Stern, Kimberlee L / Smith, Mason S / Billings, Wendy M / Loftus, Taylor J / Conover, Benjamin M / Della Corte, Dennis / Price, Joshua L

    Biochemistry

    2020  Volume 59, Issue 17, Page(s) 1672–1679

    Abstract: Here we show that a solvent- ... ...

    Abstract Here we show that a solvent-exposed
    MeSH term(s) Amino Acid Sequence ; Models, Molecular ; Peptides/chemistry ; Protein Conformation, alpha-Helical ; Protein Folding ; Protein Multimerization ; Solvents/chemistry ; Thermodynamics ; Transition Temperature
    Chemical Substances Peptides ; Solvents
    Language English
    Publishing date 2020-04-20
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.0c00045
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 217: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  5. Article: Context-Dependent Stabilizing Interactions among Solvent-Exposed Residues along the Surface of a Trimeric Helix Bundle

    Stern, Kimberlee L / Smith, Mason S / Billings, Wendy M / Loftus, Taylor J / Conover, Benjamin M / Della Corte, Dennis / Price, Joshua L

    Biochemistry. 2020 Apr. 09, v. 59, no. 17

    2020  

    Abstract: Here we show that a solvent-exposed f-position (i.e., residue 14) within a well-characterized trimeric helix bundle can facilitate a stabilizing long-range synergistic interaction involving b-position Glu10 (i.e., i – 4 relative to residue 14) and c- ... ...

    Abstract Here we show that a solvent-exposed f-position (i.e., residue 14) within a well-characterized trimeric helix bundle can facilitate a stabilizing long-range synergistic interaction involving b-position Glu10 (i.e., i – 4 relative to residue 14) and c-position Lys18 (i.e., i + 4), depending the identity of residue 14. The extent of stabilization associated with the Glu10-Lys18 pair depends primarily on the presence of a side-chain hydrogen-bond donor at residue 14; the nonpolar or hydrophobic character of residue 14 plays a smaller but still significant role. Crystal structures and molecular dynamics simulations indicate that Glu10 and Lys18 do not interact directly with each other but suggest the possibility that the proximity of residue 14 with Lys18 allows Glu10 to interact favorably with nearby Lys7. Subsequent thermodynamic experiments confirm the important role of Lys7 in the large synergistic stabilization associated with the Glu10-Lys18 pair. Our results highlight the exquisite complexity and surprising long-range synergistic interactions among b-, c-, and f-position residues within helix bundles, suggesting new possibilities for engineering hyperstable helix bundles and emphasizing the need to consider carefully the impact of substitutions at these positions for application-specific purposes.
    Keywords crystal structure ; engineering ; hydrogen bonding ; hydrophobicity ; molecular dynamics ; synergism ; thermodynamics
    Language English
    Dates of publication 2020-0409
    Size p. 1672-1679.
    Publishing place American Chemical Society
    Document type Article
    Note NAL-light
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.0c00045
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 217: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  6. Article ; Online: Cys(i)-Lys(i+3)-Lys(i+4) triad: a general approach for PEG-based stabilization of α-helical proteins.

    Pandey, Brijesh K / Smith, Mason S / Price, Joshua L

    Biomacromolecules

    2014  Volume 15, Issue 12, Page(s) 4643–4647

    Abstract: PEGylation is an important strategy for enhancing the pharmacokinetic properties of protein drugs. Modern chemoselective reactions now enable specific placement of a single PEG at any site on a protein surface. However, few rational structure-based ... ...

    Abstract PEGylation is an important strategy for enhancing the pharmacokinetic properties of protein drugs. Modern chemoselective reactions now enable specific placement of a single PEG at any site on a protein surface. However, few rational structure-based guidelines exist for selecting optimal PEGylation sites. Here, we explore the impact of PEGylation on the conformational stability of α-helices using an α-helical coiled coil as a model system. We find that maleimide-based PEGylation of a solvent-exposed i position Cys can stabilize coiled-coil quaternary structure when Lys residues occupy both the i + 3 and i + 4 positions, due to favorable interactions between the PEG-maleimide and the Lys residues. Applying this Cys(i)-Lys(i+3)-Lys(i+4) triad to a solvent-exposed position within the C-terminal helix of the villin headpiece domain leads to similar PEG-based increases in conformational stability, highlighting the possibility of using the Cys(i)-Lys(i+3)-Lys(i+4) triad as a general strategy for PEG-based stabilization of helical proteins.
    MeSH term(s) Amino Acid Sequence ; Cysteine/chemistry ; Lysine/chemistry ; Molecular Sequence Data ; Polyethylene Glycols/chemistry ; Protein Structure, Secondary ; Proteins/chemistry
    Chemical Substances Proteins ; Polyethylene Glycols (30IQX730WE) ; Lysine (K3Z4F929H6) ; Cysteine (K848JZ4886)
    Language English
    Publishing date 2014-12-08
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1526-4602
    ISSN (online) 1526-4602
    DOI 10.1021/bm501546k
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Enhancing a long-range salt bridge with intermediate aromatic and nonpolar amino acids.

    Smith, Mason S / Billings, Wendy M / Whitby, Frank G / Miller, McKenzie B / Price, Joshua L

    Organic & biomolecular chemistry

    2017  Volume 15, Issue 28, Page(s) 5882–5886

    Abstract: The interaction of a positively charged amino acid residue with a negatively charged residue (i.e. a salt bridge) can contribute substantially to protein conformational stability, especially when two ionic groups are in close proximity. At longer ... ...

    Abstract The interaction of a positively charged amino acid residue with a negatively charged residue (i.e. a salt bridge) can contribute substantially to protein conformational stability, especially when two ionic groups are in close proximity. At longer distances, this stabilizing effect tends to drop off precipitously. However, several lines of evidence suggest that salt-bridge interaction could persist at longer distances if an aromatic amino acid residue were positioned between the anion and cation. Here we explore this possibility in the context of a peptide in which a Lys residue occupies the i + 8 position relative to an i-position Glu on the solvent-exposed surface of a helix-bundle homotrimer. Variable temperature circular dichroism (CD) experiments indicate that an i + 4-position Trp enables a favorable long-range interaction between Glu and the i + 8 Lys. A substantial portion of this effect relies on the presence of a hydrogen-bond donor on the arene; however, non-polar arenes, a cyclic hydrocarbon, and an acyclic Leu side-chain can also enhance the long-range salt bridge, possibly by excluding water and ions from the space between Glu and Lys.
    Language English
    Publishing date 2017-07-19
    Publishing country England
    Document type Journal Article
    ZDB-ID 2097583-1
    ISSN 1477-0539 ; 1477-0520
    ISSN (online) 1477-0539
    ISSN 1477-0520
    DOI 10.1039/c7ob01198a
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Bulky Dehydroamino Acids Enhance Proteolytic Stability and Folding in β-Hairpin Peptides

    Jalan, Ankur / Kastner David W / Webber Kei G. I / Smith Mason S / Price Joshua L / Castle Steven L

    Organic letters. 2017 Oct. 06, v. 19, no. 19

    2017  

    Abstract: The bulky dehydroamino acids dehydrovaline (ΔVal) and dehydroethylnorvaline (ΔEnv) can be inserted into the turn regions of β-hairpin peptides without altering their secondary structures. These residues increase proteolytic stability, with ΔVal at ... ...

    Abstract The bulky dehydroamino acids dehydrovaline (ΔVal) and dehydroethylnorvaline (ΔEnv) can be inserted into the turn regions of β-hairpin peptides without altering their secondary structures. These residues increase proteolytic stability, with ΔVal at the (i + 1) position having the most substantial impact. Additionally, a bulky dehydroamino acid can be paired with a d-amino acid (i.e., d-Pro) to synergistically enhance resistance to proteolysis. A link between proteolytic stability and peptide structure is established by the finding that a stabilized ΔVal-containing β-hairpin is more highly folded than its Asn-containing congener.
    Keywords amino acids ; chemical structure ; organic compounds ; peptides ; proteolysis
    Language English
    Dates of publication 2017-1006
    Size p. 5190-5193.
    Publishing place American Chemical Society
    Document type Article
    ISSN 1523-7052
    DOI 10.1021%2Facs.orglett.7b02455
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  9. Article ; Online: Stapling of two PEGylated side chains increases the conformational stability of the WW domain via an entropic effect.

    Xiao, Qiang / Bécar, Natalie A / Brown, Nathaniel P / Smith, Mason S / Stern, Kimberlee L / Draper, Steven R E / Thompson, Katherine P / Price, Joshua L

    Organic & biomolecular chemistry

    2018  Volume 16, Issue 46, Page(s) 8933–8939

    Abstract: Hydrocarbon stapling and PEGylation are distinct strategies for enhancing the conformational stability and/or pharmacokinetic properties of peptide and protein drugs. Here we combine these approaches by incorporating asparagine-linked O-allyl PEG ... ...

    Abstract Hydrocarbon stapling and PEGylation are distinct strategies for enhancing the conformational stability and/or pharmacokinetic properties of peptide and protein drugs. Here we combine these approaches by incorporating asparagine-linked O-allyl PEG oligomers at two positions within the β-sheet protein WW, followed by stapling of the PEGs via olefin metathesis. The impact of stapling two sites that are close in primary sequence is small relative to the impact of PEGylation alone and depends strongly on PEG length. In contrast, stapling of two PEGs that are far apart in primary sequence but close in tertiary structure provides substantially more stabilization, derived mostly from an entropic effect. Comparison of PEGylation + stapling vs. alkylation + stapling at the same positions in WW reveals that both approaches provide similar overall levels of conformational stability.
    MeSH term(s) Alkenes/chemistry ; Asparagine/analogs & derivatives ; Entropy ; Models, Molecular ; Peptides/chemistry ; Polyethylene Glycols/chemistry ; Protein Conformation ; Protein Conformation, beta-Strand ; Protein Stability ; Proteins/chemistry ; WW Domains
    Chemical Substances Alkenes ; Peptides ; Proteins ; Polyethylene Glycols (3WJQ0SDW1A) ; Asparagine (7006-34-0)
    Language English
    Publishing date 2018-11-16
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2097583-1
    ISSN 1477-0539 ; 1477-0520
    ISSN (online) 1477-0539
    ISSN 1477-0520
    DOI 10.1039/c8ob02535e
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article: Cysi–Lysi+3–Lysi+4 Triad: A General Approach for PEG-Based Stabilization of α-Helical Proteins

    Pandey, Brijesh K / Smith Mason S / Price Joshua L

    Biomacromolecules. 2014 Dec. 08, v. 15, no. 12

    2014  

    Abstract: PEGylation is an important strategy for enhancing the pharmacokinetic properties of protein drugs. Modern chemoselective reactions now enable specific placement of a single PEG at any site on a protein surface. However, few rational structure-based ... ...

    Abstract PEGylation is an important strategy for enhancing the pharmacokinetic properties of protein drugs. Modern chemoselective reactions now enable specific placement of a single PEG at any site on a protein surface. However, few rational structure-based guidelines exist for selecting optimal PEGylation sites. Here, we explore the impact of PEGylation on the conformational stability of α-helices using an α-helical coiled coil as a model system. We find that maleimide-based PEGylation of a solvent-exposed i position Cys can stabilize coiled-coil quaternary structure when Lys residues occupy both the i + 3 and i + 4 positions, due to favorable interactions between the PEG-maleimide and the Lys residues. Applying this Cysᵢ–Lysᵢ₊₃–Lysᵢ₊₄ triad to a solvent-exposed position within the C-terminal helix of the villin headpiece domain leads to similar PEG-based increases in conformational stability, highlighting the possibility of using the Cysᵢ–Lysᵢ₊₃–Lysᵢ₊₄ triad as a general strategy for PEG-based stabilization of helical proteins.
    Keywords chemical bonding ; drugs ; guidelines ; models ; pharmacokinetics ; proteins
    Language English
    Dates of publication 2014-1208
    Size p. 4643-4647.
    Publishing place American Chemical Society
    Document type Article
    ISSN 1526-4602
    DOI 10.1021%2Fbm501546k
    Database NAL-Catalogue (AGRICOLA)

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