Collagen-Binding Peptide Interaction with Retinal Tissue Surfaces

Sistiabudi, Rizaldi; Ivanisevic, Albena

doi:10.1021/la703561d

Cited by 23 publications

(32 citation statements)

References 18 publications

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“…The surface of the ICL is primarily composed of collagen type I and type III. The capacity of the collagen binding sequence to bind both types of collagen has been confirmed in our previous study (Sistiabudi and Ivanisevic 2008). Thus in the binding specificity study, only type I collagen was used.…”

Section: Fluorescent Binding Assaymentioning

confidence: 80%

“…We have previously reported that the surface of the inner collagenous layer (ICL) is composed of well-defined collagen fibers. Further, we have identified them as collagen type I and type III (Sistiabudi and Ivanisevic 2008). With this in mind, we proposed a strategy employing a collagen-binding peptide sequence to anchor bioactive molecules on the ICL surface.…”

Section: Introductionmentioning

confidence: 98%

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Modification of native collagen with cell‐adhesive peptide to promote RPE cell attachment on Bruch's membrane

Sistiabudi

Paderi

Panitch

et al. 2008

Biotech & Bioengineering

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Current efforts to reverse loss of visual function due to Age-related Macular Degeneration point to the restoration of the Retinal Pigment Epithelial (RPE) layer. Restoration of the RPE layer involves replacing lost RPE cells as well as addressing the degeneration of the underlying Bruch's membrane (BM). To advance the potential of using donor BM, we present a strategy to achieve specific and controllable modification of the inner collagenous layer (ICL) of the Bruch's membrane. In particular, interaction between a collagen binding peptide (CBP) sequence with exposed collagen fibers on the ICL surface is utilized to anchor bioactive molecules. Here, a cell-adhesion sequence is added to the collagen binding sequence to promote attachment and survival of ARPE-19. First, the binding specificity of the CBP sequence is verified with a fluorescent binding assay. Subsequently, the effect of modification using the peptide is studied qualitatively using confocal fluorescent imaging and quantitatively through a cell proliferation assay. Results of these experiments indicate that the peptide sequence binds specifically to collagen fibers. Additionally, modification using the peptide enhanced cell adhesion, allowing large uniform cell networks to be formed on the surface. Furthermore, modification with the peptide also delayed the onset of apoptosis on adherent cells.

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Section: Fluorescent Binding Assaymentioning

confidence: 80%

Section: Introductionmentioning

confidence: 98%

Modification of native collagen with cell‐adhesive peptide to promote RPE cell attachment on Bruch's membrane

Sistiabudi

Paderi

Panitch

et al. 2008

Biotech & Bioengineering

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“…The collagen-binding peptide (CBP) is a collagen-binding fragment derived from fibronectin and has previously been shown to bind to Bruch's membrane. 14,20 Our FT-IR data indicates that this fragment dramatically changes its secondary structure after contact with the collagen substrate. Prior to binding, the CBP has primarily a parallel β-sheet secondary structure (Figure 4, an amide I peak at 1638 cm -1 and amide II peaks at 1539 cm -1 ).…”

Section: Resultsmentioning

confidence: 94%

Characterization of Conformational Adsorbate Changes on a Tissue-Derived Substrate Using Fourier Transform Infrared Spectroscopy

Kramer

Andrews²,

Hugar

et al. 2010

Langmuir

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Fourier transform infrared (FT-IR) spectroscopy is utilized to observe adsorbate interactions with a tissue-derived collagen scaffold extracted from the Bruch's membrane of pig eyes. The characterization includes conformational changes in isoleucine, polyisoleucine, collagen-binding peptide, RGD-tagged collagen-binding peptide, and laminin after adsorption onto the substrate. Isotopically labeled isoleucine is further utilized to understand changes in the biomolecular structure upon binding to a tissue-derived surface. The adsorbates associated with the collagen scaffold predominately through hydrophobic interactions and hydrogen bonding. The results of this study can be used to improve our understanding of surface chemistry changes during the engineering of biomimetic scaffolds before and after biomolecule adsorption.

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“…Two CMP sequences were used in these studies: GPP: (GPP) 3 GPRGEKGERGPR(GPP) 3 GPCCG GPO: (GPO) 4 GEKGER(GPO) 4 GGGG A scrambled GPO sequence, shown not to form a triple helix, was used as a control. Both CMPs were retained when preheated above their melting temperatures (T m ).…”

Section: A Cmp Retention Studiesmentioning

confidence: 99%

The modification of collagen scaffolds for application in regenerative medicine

Urello

Sullivan

Kiick

2014

2014 40th Annual Northeast Bioengineering Conference (NEBEC)

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The use of collagen-based biomaterials in regenerative medicine has rapidly increased over the past decade. Over this period, a variety of collagen modification techniques have been developed for the purpose of retaining therapeutics. Most techniques rely on chemical treatments, but a biomimetic strategy to noncovalently modify collagen scaffolds with collagen mimetic peptides (CMPs) offers compelling advantages. The goal of this project is to create a stable, tunable collagen-based delivery system using a simple peptide-based strategy that retains collagen bioactivity. This study will be one of the first to thoroughly examine the controllability of nanoparticle release through variation of CMP sequence and CMP density on nanoparticles, and to modify collagen with nanoparticles utilizing a non-GPO-based, potentially mass-producible CMP. Currently, one GPO-and one GPP-based peptide have been synthesized, and their ability to be retained on a collagen scaffold under physiological conditions for over a week has been demonstrated. The incorporation of CMPs onto nanoparticles has also been found to enable retention on collagen scaffolds for similar periods of time, and our recent findings suggest that CMP sequence and density directly affect the release rate. In the future, we will continue to focus on varying both CMP sequence and density to attain release profiles consistent with wound repair kinetics.

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Collagen-Binding Peptide Interaction with Retinal Tissue Surfaces

Cited by 23 publications

References 18 publications

Modification of native collagen with cell‐adhesive peptide to promote RPE cell attachment on Bruch's membrane

Modification of native collagen with cell‐adhesive peptide to promote RPE cell attachment on Bruch's membrane

Characterization of Conformational Adsorbate Changes on a Tissue-Derived Substrate Using Fourier Transform Infrared Spectroscopy

The modification of collagen scaffolds for application in regenerative medicine

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