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  1. Article: Storage Stability Study of Salicylate-based Poly(anhydride-esters).

    Deronde, Brittany M / Carbone, Ashley L / Uhrich, Kathryn E

    Polymer degradation and stability

    2010  Volume 95, Issue 9, Page(s) 1778–1782

    Abstract: Storage stability was evaluated on a biodegradable salicylate-based poly(anhydride-ester) to elucidate the effects of storage conditions over time. The hydrolytically labile polymer samples were stored in powdered form at five relevant storage ... ...

    Abstract Storage stability was evaluated on a biodegradable salicylate-based poly(anhydride-ester) to elucidate the effects of storage conditions over time. The hydrolytically labile polymer samples were stored in powdered form at five relevant storage temperatures (-12 °C, 4 °C, 27 °C, 37 °C, 50 °C) and monitored over four weeks for changes in color, glass transition temperature, molecular weight, and extent of hydrolysis. Samples stored at lower temperatures remained relatively constant with respect to bond hydrolysis and molecular weight. Whereas, samples stored at higher temperatures displayed significant hydrolysis. For hydrolytically degradable polymers, such as these poly(anhydride-esters), samples are best stored at low temperatures under an inert atmosphere.
    Language English
    Publishing date 2010-11-30
    Publishing country England
    Document type Journal Article
    ZDB-ID 1502217-1
    ISSN 0141-3910
    ISSN 0141-3910
    DOI 10.1016/j.polymdegradstab.2010.05.008
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Designing mimics of membrane active proteins.

    Sgolastra, Federica / Deronde, Brittany M / Sarapas, Joel M / Som, Abhigyan / Tew, Gregory N

    Accounts of chemical research

    2013  Volume 46, Issue 12, Page(s) 2977–2987

    Abstract: As a semipermeable barrier that controls the flux of biomolecules in and out the cell, the plasma membrane is critical in cell function and survival. Many proteins interact with the plasma membrane and modulate its physiology. Within this large landscape ...

    Abstract As a semipermeable barrier that controls the flux of biomolecules in and out the cell, the plasma membrane is critical in cell function and survival. Many proteins interact with the plasma membrane and modulate its physiology. Within this large landscape of membrane-active molecules, researchers have focused significant attention on two specific classes of peptides, antimicrobial peptides (AMPs) and cell penetrating peptides (CPPs), because of their unique properties. In this Account, we describe our efforts over the last decade to build and understand synthetic mimics of antimicrobial peptides (SMAMPs). These endeavors represent one specific example of a much larger effort to understand how synthetic molecules interact with and manipulate the plasma membrane. Using both defined molecular weight oligomers and easier to produce, but heterogeneous, polymers, we have generated scaffolds with biological potency exceeding that of the natural analogues. One of these compounds has progressed through a phase II clinical trial for pan-staph infections. Modern biophysical assays have highlighted the interplay between the synthetic scaffold and lipid composition: a negative Gaussian curvature is required both for pore formation and for the initiation of endosome creation. Although work remains to better resolve the complexity of this interplay between lipids, other bilayer components, and the scaffolds, significant new insights have been discovered. These results point to the importance of considering the various aspects of permeation and how these are related to "pore formation". More recently, our efforts have expanded toward protein transduction domains, or mimics of cell penetrating peptides. Using a combination of unique molecular scaffolds and guanidinium-rich side chains, we have produced an array of polymers with robust membrane (and delivery) activity. In this new area, researchers are just beginning to understand the fundamental interactions between these new scaffolds and the plasma membrane. Negative Gaussian curvature is also important in these systems, but the detailed relationships between molecular structure, self-assembly with lipids, and translocation will require more investigation. It has become clear that the combination of molecular design, biophysical models, and biological evaluation provides a robust approach to the generation and study of novel proteinomimetics.
    MeSH term(s) Antimicrobial Cationic Peptides/chemical synthesis ; Antimicrobial Cationic Peptides/chemistry ; Biomimetics ; Drug Design ; Membrane Proteins/chemistry ; Molecular Structure
    Chemical Substances Antimicrobial Cationic Peptides ; Membrane Proteins
    Language English
    Publishing date 2013-09-05
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1483291-4
    ISSN 1520-4898 ; 0001-4842
    ISSN (online) 1520-4898
    ISSN 0001-4842
    DOI 10.1021/ar400066v
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

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