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  • 1. Gunasekera, S.
    et al.
    Fernandes-Cerqueira, C.
    Wennmalm, Stefan
    KTH, School of Engineering Sciences (SCI), Applied Physics, Experimental Biomolecular Physics. KTH, Centres, Science for Life Laboratory, SciLifeLab.
    Wähämaa, H.
    Sommarin, Y.
    Catrina, A. I.
    Jakobsson, P. -J
    Göransson, U.
    Stabilized Cyclic Peptides as Scavengers of Autoantibodies: Neutralization of Anticitrullinated Protein/Peptide Antibodies in Rheumatoid Arthritis2018In: ACS Chemical Biology, ISSN 1554-8929, E-ISSN 1554-8937, Vol. 13, no 6, p. 1525-1535Article in journal (Refereed)
    Abstract [en]

    The occurrence of autoantibodies is a hallmark of rheumatoid arthritis, specifically those autoantibodies targeting proteins containing the arginine-derived amino acid citrulline. There is strong evidence showing that the occurrence of anticitrullinated protein/peptide antibodies (ACPA) are involved in disease progression, and ACPA was recently shown to induce pain in animals. Here, we explore a novel concept useful for research, diagnostics, and possibly therapy of autoimmune diseases, namely, to directly target and neutralize autoantibodies using peptide binders. A high-affinity peptide-based scavenger of ACPA was developed by grafting a citrullinated epitope derived from human fibrinogen into a naturally occurring stable peptide scaffold. The best scavenger comprises the truncated epitope α-fibrinogen, [Cit573]fib(566-580), grafted into the scaffold sunflower trypsin inhibitor-1, SFTI-1. The final peptide demonstrates low nanomolar apparent affinity and superior stability.

  • 2. Rahman, M. Mahafazur
    et al.
    Zetterberg, Henrik
    Lendel, Christofer
    Swedish University of Agricultural Sciences (SLU), Sweden .
    Hard, Torleif
    Binding of Human Proteins to Amyloid-beta Protofibrils2015In: ACS Chemical Biology, ISSN 1554-8929, E-ISSN 1554-8937, Vol. 10, no 3, p. 766-774Article in journal (Refereed)
    Abstract [en]

    The progressive neurodegeneration in Alzheimers disease is believed to be linked to the presence of prefibrillar aggregates of the amyloid-beta (A beta) peptide in the brain. The exact role of these aggregates in the disease pathology is, however, still an open question. Any mechanism by which oligomeric A beta may cause damage to neuronal cells must, in one way or another, involve interactions with other molecules. Here, we identify proteins in human serum and cerebrospinal fluid that bind to stable protofibrils formed by an engineered variant of A beta 42 (A beta(42CC)). We find that the protofibrils attract a substantial number of protein binding partners. Many of the 101 identified proteins are involved in lipid transport and metabolism, the complement system, or in hemostasis. Binding of representative proteins from all of these groups with micromolar affinity was confirmed using surface plasmon resonance. In addition, binding of apolipoprotein E to the protofibrils with nanomolar affinity was demonstrated. We also find that aggregation of A beta enhances protein binding, as lower amounts of proteins bind monomeric A beta. Proteins that bind to A beta protofibrils might contribute to biological effects in which these aggregates are involved. Our results therefore suggest that an improved understanding of the mechanisms by which A beta causes cytotoxicity and neurodegeneration might be gained from studies carried out in biologically relevant matrices in which A beta-binding proteins are present.

  • 3.
    Storti, Barbara
    et al.
    Scuola Normale Super Pisa, NEST, I-56127 Pisa, Italy.;NANO CNR, I-56127 Pisa, Italy..
    Margheritis, Eleonora
    Ist Italiano Tecnol, Ctr Nanotechnol Innovat NEST, I-56127 Pisa, Italy..
    Abbandonato, Gerardo
    Scuola Normale Super Pisa, NEST, I-56127 Pisa, Italy.;NANO CNR, I-56127 Pisa, Italy..
    Domenichini, Giorgio
    Scuola Normale Super Pisa, NEST, I-56127 Pisa, Italy.;NANO CNR, I-56127 Pisa, Italy..
    Dreier, Jes
    KTH, School of Engineering Sciences (SCI), Applied Physics. KTH, Centres, Science for Life Laboratory, SciLifeLab.
    Testa, Ilaria
    KTH, School of Engineering Sciences (SCI), Applied Physics. KTH, Centres, Science for Life Laboratory, SciLifeLab.
    Garau, Gianpiero
    Ist Italiano Tecnol, Ctr Nanotechnol Innovat NEST, I-56127 Pisa, Italy..
    Nifosi, Riccardo
    Scuola Normale Super Pisa, NEST, I-56127 Pisa, Italy.;NANO CNR, I-56127 Pisa, Italy..
    Bizzarri, Ranieri
    Scuola Normale Super Pisa, NEST, I-56127 Pisa, Italy.;NANO CNR, I-56127 Pisa, Italy..
    Role of Gln222 in Photoswitching of Aequorea Fluorescent Proteins: A Twisting and H-Bonding Affair?2018In: ACS Chemical Biology, ISSN 1554-8929, E-ISSN 1554-8937, Vol. 13, no 8, p. 2082-2093Article in journal (Refereed)
    Abstract [en]

    Reversibly photoswitchable fluorescent proteins (RSFPs) admirably combine the genetic encoding of fluorescence with the ability to repeatedly toggle between a bright and dark state, adding a new,temporal dimension to the fluorescence signal. Accordingly, in recent years RSFPs have paved the way to novel applications in cell imaging that rely on their reversible photoswitching, including many super-resolution techniques such as F-PALM, RESOLFT, and SOFI that provide nanoscale pictures of the living matter. Yet many RSFPs have been engineered by a rational approach only to a limited extent, in the absence of clear structure property relationships that in most cases make anecdotic the emergence of the photoswitching. We reported [Bizzarri et al. J. Am Chem Soc. 2010, 102, 85] how the E222Q replacement is a single photoswitching mutation, since it restores the intrinsic cis-trans photo-isomerization properties of the chromophore in otherwise nonswitchable Aequorea proteins of different color and mutation pattern (Q-RSFPs). We here investigate the subtle role of Q222 on the excited-state photophysics of the two simplest Q-RSFPs by a combined experimental and theoretical approach, using their nonswitchable anacestor EGFP as benchmark. Our findings link indissolubly photoswitching and Q222 presence, by a simple yet elegant scenario: largely twisted chromophore structures around the double bond (including hula-twist configurations) are uniquely stabilized by Q222 via H-bonds. Likely, these H-bonds subtly modulate the electronic properties of the chromophore, enabling the conical intersection that connects the excited cis to ground trans chromophore. Thus, Q222 belongs to a restricted family of single mutations that change dramatically the functional phenotype of a protein. The capability to distinguish quantitatively T65S/E222Q EGFP ("WildQ", wQ) from the spectrally identical EGFP by quantitative Optical Lock-In Detection (qOLID) witnesses the relevance of this mutation for cell imaging.

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