Search results for: Barbara Brodsky

Items from 1 to 20 out of 48 results

article

Effects of flexibility of the α2 chain of type I collagen on collagenase cleavage

Arya Mekkat, Erik Poppleton, Bo An, Robert Visse, more

Journal of Structural Biology > 2018 > 203 > 3 > 247-254

Cleavage of collagen by collagenases such as matrix metalloproteinase 1 (MMP-1) is a key step in development, tissue remodeling, and tumor proliferation. The abundant heterotrimeric type I collagen composed of two α1(I) chains and one α2(I) chain is efficiently cleaved by MMP-1 at a unique site in the triple helix, a process which may be initiated by local unfolding within the peptide chains. Atypical...

article

Collagen Gly missense mutations: Effect of residue identity on collagen structure and integrin binding

Yimin Qiu, Arya Mekkat, Hongtao Yu, Sezin Yigit, more

Journal of Structural Biology > 2018 > 203 > 3 > 255-262

Gly missense mutations in type I collagen, which replace a conserved Gly in the repeating (Gly-Xaa-Yaa)_n sequence with a larger residue, are known to cause Osteogenesis Imperfecta (OI). The clinical consequences of such mutations range from mild to lethal, with more serious clinical severity associated with larger Gly replacement residues. Here, we investigate the influence of the identity of the...

article

Collagen interactions: Drug design and delivery

Bo An, Yu-Shan Lin, Barbara Brodsky

Advanced Drug Delivery Reviews > 2016 > 97 > C > 69-84

Collagen is a major component in a wide range of drug delivery systems and biomaterial applications. Its basic physical and structural properties, together with its low immunogenicity and natural turnover, are keys to its biocompatibility and effectiveness. In addition to its material properties, the collagen triple-helix interacts with a large number of molecules that trigger biological events. Collagen...

article

Bacterial collagen-like proteins that form triple-helical structures

Zhuoxin Yu, Bo An, John A.M. Ramshaw, Barbara Brodsky

Journal of Structural Biology > 2014 > 186 > 3 > 451-461

A large number of collagen-like proteins have been identified in bacteria during the past 10years, principally from analysis of genome databases. These bacterial collagens share the distinctive Gly-Xaa-Yaa repeating amino acid sequence of animal collagens which underlies their unique triple-helical structure. A number of the bacterial collagens have been expressed in Escherichia coli, and they all...

article

Active Learning Approaches for Nutrition Education in the Medical School Curriculum

Sangita Phadtare, James Galt, Barbara Brodsky

Medical Science Educator > 2014 > 24 > 1 > 27-33

We designed and implemented several active learning approaches at our medical school to stimulate student interest in nutrition and to help them feel more comfortable and competent in talking about nutrition. Positive feedback and overall engagement of students suggested that these approaches stimulated their interest in basic aspects of nutrition.

article

The Role of Cross-Chain Ionic Interactions for the Stability of Collagen Model Peptides

Neelam Keshwani, Shounak Banerjee, Barbara Brodsky, George I. Makhatadze

Biophysical Journal > 2013 > 105 > 7 > 1681-1688

The contribution of ionic interactions to the stability of the collagen triple helix was studied using molecular dynamics (MD) simulations and biophysical methods. To this end, we examined the stability of a host-guest collagen model peptide, Ac-GPOGPOGPYGXOGPOGPO-NH₂, substituting KGE, KGD, EGK, and DGK for the YGX sequence. All-atom, implicit solvent MD simulations show that the fraction of cross-chain...

article

The influence of specific binding of collagen–silk chimeras to silk biomaterials on hMSC behavior

Bo An, Teresa M. DesRochers, Guokui Qin, Xiaoxia Xia, more

Biomaterials > 2013 > 34 > 2 > 402-412

Collagen-like proteins in the bacteria Streptococcus pyogenes adopt a triple-helix structure with a thermal stability similar to that of animal collagens, can be expressed in high yield in Escherichia coli and can be easily modified through molecular biology techniques. However, potential applications for such recombinant collagens are limited by their lack of higher order structure to achieve the...

article

A peptide study of the relationship between the collagen triple‐helix and amyloid

Avanish S. Parmar, Ana Monica Nunes, Jean Baum, Barbara Brodsky

Biopolymers > 97 > 10 > 795 - 806

Type XXV collagen, or collagen‐like amyloidogenic component, is a component of amyloid plaques, and recent studies suggest this collagen affects amyloid fibril elongation and has a genetic association with Alzheimer's disease. The relationship between the collagen triple helix and amyloid fibrils was investigated by studying peptide models, including a very stable triple helical peptide (Pro‐Hyp‐Gly)...

article

Osteogenesis Imperfecta Missense Mutations in Collagen: Structural Consequences of a Glycine to Alanine Replacement at a Highly Charged Site

Jianxi Xiao, Haiming Cheng, Teresita Silva, Jean Baum, more

Biochemistry > 2011 > 50 > 50 > 10771 - 10780

article

Uv damage of collagen: Insights from model collagen peptides

Ketevan Jariashvili, Balaraman Madhan, Barbara Brodsky, Ana Kuchava, more

Biopolymers > 97 > 3 > 189 - 198

Fibrils of Type I collagen in the skin are exposed to ultraviolet (UV) light and there have been claims that collagen photo‐degradation leads to wrinkles and may contribute to skin cancers. To understand the effects of UV radiation on collagen, Type I collagen solutions were exposed to the UV‐C wavelength of 254 nm for defined lengths of time at 4°C. Circular dichroism (CD) experiments show that irradiation...

article

Osteogenesis Imperfecta Model Peptides: Incorporation of Residues Replacing Gly within a Triple Helix Achieved by Renucleation and Local Flexibility

Jianxi Xiao, Balaraman Madhan, Yingjie Li, Barbara Brodsky, more

Biophysical Journal > 2011 > 101 > 2 > 449-458

Missense mutations, which replace one Gly with a larger residue in the repeating sequence of the type I collagen triple helix, lead to the hereditary bone disorder osteogenesis imperfecta (OI). Previous studies suggest that these mutations may interfere with triple-helix folding. NMR was used to investigate triple-helix formation in a series of model peptides where the residue replacing Gly, as well...

article

Sequence environment of mutation affects stability and folding in collagen model peptides of osteogenesis imperfecta

Michael A. Bryan, Haiming Cheng, Barbara Brodsky

Biopolymers > 96 > 1 > 4 - 13

Osteogenesis imperfecta (OI), a disorder characterized by fragile bones, is often a consequence of missense mutations in type I collagen, which change one Gly in the repeating (Gly‐Xaa‐Yaa)_n sequence to a larger amino acid. The impact of local environment and the identity of the residue replacing Gly were investigated using two sets of triple‐helical peptides. Gly mutations in the highly stable (Pro‐Hyp‐Gly)...

article

A Streptococcus pyogenes derived collagen-like protein as a non-cytotoxic and non-immunogenic cross-linkable biomaterial

Yong Y. Peng, Ayumi Yoshizumi, Stephen J. Danon, Veronica Glattauer, more

Biomaterials > 2010 > 31 > 10 > 2755-2761

A range of bacteria have been shown to contain collagen-like sequences that form triple-helical structures. Some of these proteins have been shown to form triple-helical motifs that are stable around body temperature without the inclusion of hydroxyproline or other secondary modifications to the protein sequence. This makes these collagen-like proteins particularly suitable for recombinant production...

article

Expanding the Family of Collagen Proteins: Recombinant Bacterial Collagens of Varying Composition Form Triple-Helices of Similar Stability

Chunying Xu, Zhuoxin Yu, Masayori Inouye, Barbara Brodsky, more

Biomacromolecules > 2010 > 11 > 2 > 348 - 356

article

Investigation of Collagen Glycine Substitution Mutations Leading to Disease in a Bacteria Collagen System and Collagen Like Peptides

Haiming Cheng, Shayan Rashid, Zhuoxin Yu, Ayumi Yoshizumi, more

Biophysical Journal > 2010 > 98 > 3 Supplement 1 > 446a

article

Triple-Helix Folding Around Interruptions in the Collagen Repeating Sequence

Eileen Hwang, Barbara Brodsky

Biophysical Journal > 2010 > 98 > 3 Supplement 1 > 32a

article

Aromatic Interactions Promote Self-Association of Collagen Triple-Helical Peptides to Higher-Order Structures

Karunakar Kar, Sajjad Ibrar, Vikas Nanda, Todd M. Getz, more

Biochemistry > 2009 > 48 > 33 > 7959 - 7968

article

High expression and physical properties of bacterial collagen

Ayumi Yoshizumi, Zhuoxin Yu, Geetha Thiagarajan, Teresita Silva, more

Matrix Biology > 2008 > 27 > Supplement 1 > 53

article

NMR Monitoring of Chain-Specific Stability in Heterotrimeric Collagen Peptides

Balaraman Madhan, Jianxi Xiao, Geetha Thiagarajan, Jean Baum, more

Journal of the American Chemical Society > 2008 > 130 > 41 > 13520 - 13521

article

Predicting the Clinical Lethality of Osteogenesis Imperfecta from Collagen Glycine Mutations ^†

Dale L. Bodian, Balaraman Madhan, Barbara Brodsky, Teri E. Klein

Biochemistry > 2008 > 47 > 19 > 5424 - 5432

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INFONA - science communication portal

Search results for: Barbara Brodsky

Effects of flexibility of the α2 chain of type I collagen on collagenase cleavage

Collagen Gly missense mutations: Effect of residue identity on collagen structure and integrin binding

Collagen interactions: Drug design and delivery

Bacterial collagen-like proteins that form triple-helical structures

Active Learning Approaches for Nutrition Education in the Medical School Curriculum

The Role of Cross-Chain Ionic Interactions for the Stability of Collagen Model Peptides

The influence of specific binding of collagen–silk chimeras to silk biomaterials on hMSC behavior

A peptide study of the relationship between the collagen triple‐helix and amyloid

Osteogenesis Imperfecta Missense Mutations in Collagen: Structural Consequences of a Glycine to Alanine Replacement at a Highly Charged Site

Uv damage of collagen: Insights from model collagen peptides

Osteogenesis Imperfecta Model Peptides: Incorporation of Residues Replacing Gly within a Triple Helix Achieved by Renucleation and Local Flexibility

Sequence environment of mutation affects stability and folding in collagen model peptides of osteogenesis imperfecta

A Streptococcus pyogenes derived collagen-like protein as a non-cytotoxic and non-immunogenic cross-linkable biomaterial

Expanding the Family of Collagen Proteins: Recombinant Bacterial Collagens of Varying Composition Form Triple-Helices of Similar Stability

Investigation of Collagen Glycine Substitution Mutations Leading to Disease in a Bacteria Collagen System and Collagen Like Peptides

Triple-Helix Folding Around Interruptions in the Collagen Repeating Sequence

Aromatic Interactions Promote Self-Association of Collagen Triple-Helical Peptides to Higher-Order Structures

High expression and physical properties of bacterial collagen

NMR Monitoring of Chain-Specific Stability in Heterotrimeric Collagen Peptides

Predicting the Clinical Lethality of Osteogenesis Imperfecta from Collagen Glycine Mutations ^†

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