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Cross-beta structure comprising amyloid-binding proteins and methods for detection of the cross-beta structure, for modulating cross-beta structures fibril formation and for modulating cross-beta structure-mediated toxicity

a cross-beta and protein technology, applied in the field of biotechnology, biochemistry, molecular biology, structural biology and medicine, can solve the problems of unknowing the why and how of all of these proteins, and achieve the effect of increasing local cytotoxicity and/or fibrinolysis

Inactive Publication Date: 2006-03-02
CROSSBETA BIOSCIENCES BV
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Moreover, it was unknown why and how all of these proteins, which lack primary sequence homology, bind tPA.

Method used

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  • Cross-beta structure comprising amyloid-binding proteins and methods for detection of the cross-beta structure, for modulating cross-beta structures fibril formation and for modulating cross-beta structure-mediated toxicity
  • Cross-beta structure comprising amyloid-binding proteins and methods for detection of the cross-beta structure, for modulating cross-beta structures fibril formation and for modulating cross-beta structure-mediated toxicity
  • Cross-beta structure comprising amyloid-binding proteins and methods for detection of the cross-beta structure, for modulating cross-beta structures fibril formation and for modulating cross-beta structure-mediated toxicity

Examples

Experimental program
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Effect test

example 1

Reagents

[0105] Bovine serum albumin (BSA) fraction V pH 7.0 and D-glucose-6-phosphate di-sodium (g6p), D, L-glyceraldehyde, and chicken egg-white lysozyme were from ICN (Aurora, Ohio, USA). Rabbit anti-recombinant tissue-type plasminogen activator (tPA) 385R and mouse anti-recombinant tPA 374B were purchased from American Diagnostica (Veenendaal, The Netherlands). Anti-laminin (L9393) was from Sigma. Swine anti-rabbit immunoglobulins / HRP (SWARPO) and rabbit anti-mouse immunoglobulins / HRP (RAMPO) were from DAKO Diagnostics B.V. (The Netherlands). Alteplase (recombinant tissue-type plasminogen activator, tPA) was obtained from Boehringer-Ingelheim (Germany). Reteplase (Rapilysin), a recombinant mutant tPA containing only kringle 2 and the catalytic domain (K2P-tPA) was obtained from Roche, Hertfordshire, UK, and porcine pancreas carboxypeptidase B (CpB) was from Roche, Mannheim, Germany. Carboxypeptidase inhibitor (CPI) was from Calbiochem (La Jolla, Calif., USA). Tween 20 was purcha...

example 2

Synthetic Peptides

[0106] Peptide Aβ (1-40), containing amino acids as present in the described human Alzheimer peptide (DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV) (SEQ ID NO: 18), fibrin peptides 85 (or FP13) (KRLEVDIDIKIRS) (SEQ ID NO: 19), 86 (or FP12) (KRLEVDIDIKIR) (SEQ ID NO: 20) and 87 (or FP10) (KRLEVDIDIK) (SEQ ID NO: 21), derived from the sequence of human fibrin(ogen) and the islet amyloid polypeptide (IAPP) peptide or derivatives (fl-hIAPP: KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY (SEQ ID NO: 22), ΔhIAPP (SNNFGAILSS) (SEQ ID NO:23 ), ΔmIAPP (SNNLGPVLPP) (SEQ ID NO: 24) were obtained from Pepscan, Inc. (The Netherlands) or from the peptide synthesis facility at the Netherlands Cancer Institute (NCI, Amsterdam, The Netherlands). The peptides were dissolved in phosphate buffered saline (PBS) to a final concentration of 1 mg ml−1 and stored for three weeks at room temperature (RT) to allow formation of fibrils. During this period, the suspension was vortexed twice weekly. After ...

example 3

Congo Red Binding and Thioflavin T Fluorescence of a Fibrin Clot

[0107] For Thioflavin T-fluorescence measurements, 1 mg ml−1 of fibrinogen was incubated at 37° C. with 2 U ml−1 of factor IIa in 150 mM NaCl, 20 mM Tris-HCl pH 7.5, 10 mM CaCl2, 50 μM Thioflavin T. Background fluorescence of a clot was recorded in the absence of Thioflavin T and background Thioflavin T fluorescence was measured in the absence of factor IIa. Fluorescence was measured on a Hitachi F-4500 fluorescence spectrophotometer (Ltd., Tokyo, Japan), using Sarstedt REF67.754 cuvettes. Apparatus settings: excitation at 435 nm (slit 10 nm), emission at 485 nm (slit 10 nm), PMT voltage 950 V, measuring time 10 seconds, delay 0 seconds. For detection of Congo red binding, a fibrin clot was formed at room temperature as described above (Thioflavin T was omitted in the buffer). The clot was incubated with Congo red solution and washed according to the manufacturer's recommendations (Sigma Diagnostics, MO, USA). The clot...

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Abstract

The invention relates to the field of biochemistry, molecular biology, structural biology and medicine. More in particular, the invention relates to cross-β structures and the biological role of these cross-β structures. In one embodiment, the invention discloses a method for modulating extracellular protein degradation and / or protein clearance comprising modulating cross-β(beta) structure formation (and / or cross-β structure-mediated activity) of the protein present in the circulation.

Description

CROSS-REFERENCE TO RELATED APPLICATIONS [0001] This application is a continuation of PCT International Patent Application PCT / NL2003 / 000501, filed Jul. 8, 2003, designating the United States of America, corresponding to PCT International Publication WO 2004 / 004698 A3 (published in English on Jan. 15, 2004), the contents of the entirety of which are incorporated by this reference.TECHNICAL FIELD [0002] The invention relates to the fields of biotechnology, biochemistry, molecular biology, structural biology and medicine. More in particular, the invention relates to cross-β structure, their binding proteins and their biological roles. BACKGROUND [0003] An increasing body of evidence suggests that unfolding of globular proteins can lead to toxicity.1 Unfolded proteins can initiate protein aggregation and fibrillization by adopting a partially structured conformation. Such fibrillar aggregates can (slowly) accumulate in various tissue types and are associated with a variety of degenerati...

Claims

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Application Information

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Patent Type & Authority Applications(United States)
IPC IPC(8): A61K8/96G01N33/53A61K38/48A61K31/00A61K31/195G01N33/50A61K31/197A61K31/198A61K31/7004A61K38/00A61K38/49A61K39/395A61K45/00A61P3/10A61P7/02A61P7/04A61P9/10A61P25/00A61P25/08A61P25/16A61P25/28A61P29/00A61P31/00A61P31/04A61P35/00A61P37/00A61P37/06C12N9/72G01N33/15G01N33/68
CPCA61K31/00C12Y304/21069A61K31/197A61K31/198A61K31/7004A61K38/49C07K16/18C07K2319/23C12N9/6459G01N33/6854G01N33/6896G01N2333/9726G01N2800/042G01N2800/2821A61K31/195A61P19/00A61P19/02A61P25/00A61P25/08A61P25/16A61P25/28A61P29/00A61P3/00A61P3/10A61P31/00A61P31/04A61P35/00A61P37/00A61P37/06A61P7/00A61P7/02A61P7/04A61P9/00A61P9/10
Inventor KROON-BATENBURG, LOUISEBOUMA, BARENDKRANENBURG, ONNOGEBBINK, MARTIJN FRANS BEN GERARD
Owner CROSSBETA BIOSCIENCES BV
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