Title: insoluble proteins catch heterologous soluble proteins into inclusion bodies by intermolecular interaction of aggregating peptides

[1]  Amy K. Cain,et al.  An amphipathic peptide with antibiotic activity against multidrug-resistant Gram-negative bacteria , 2020, Nature Communications.

[2]  X. Daura,et al.  Aggregation-prone peptides modulate activity of bovine interferon gamma released from naturally occurring protein nanoparticles. , 2020, New biotechnology.

[3]  E. Vázquez,et al.  Engineering Secretory Amyloids for Remote and Highly Selective Destruction of Metastatic Foci , 2019, Advanced materials.

[4]  S. Straus,et al.  Mechanisms of Action for Antimicrobial Peptides With Antibacterial and Antibiofilm Functions , 2019, Front. Microbiol..

[5]  O. Spadiut,et al.  Boosting Recombinant Inclusion Body Production—From Classical Fed-Batch Approach to Continuous Cultivation , 2019, Front. Bioeng. Biotechnol..

[6]  Frederic D. Schramm,et al.  Protein aggregation in bacteria , 2019, FEMS microbiology reviews.

[7]  A. Arciello,et al.  Cost-effective production of recombinant peptides in Escherichia coli. , 2019, New biotechnology.

[8]  U. Rinas,et al.  Targeting Antitumoral Proteins to Breast Cancer by Local Administration of Functional Inclusion Bodies , 2019, Advanced science.

[9]  Valentin Iglesias,et al.  Aggrescan3D (A3D) 2.0: prediction and engineering of protein solubility , 2019, Nucleic Acids Res..

[10]  W. Wiechert,et al.  Tailoring the properties of (catalytically)-active inclusion bodies , 2019, Microbial Cell Factories.

[11]  O. Spadiut,et al.  Perspectives of inclusion bodies for bio-based products: curse or blessing? , 2018, Applied Microbiology and Biotechnology.

[12]  Oliver Spadiut,et al.  Inclusion Body Bead Size in E. coli Controlled by Physiological Feeding , 2018, Microorganisms.

[13]  E. Vázquez,et al.  Release of targeted protein nanoparticles from functional bacterial amyloids: A death star‐like approach , 2018, Journal of controlled release : official journal of the Controlled Release Society.

[14]  Jayachandran N. Kizhakkedathu,et al.  Antimicrobial Peptides: Diversity, Mechanism of Action and Strategies to Improve the Activity and Biocompatibility In Vivo , 2018, Biomolecules.

[15]  Sophie E Jackson,et al.  Factors affecting the physical stability (aggregation) of peptide therapeutics , 2017, Interface Focus.

[16]  Esther Vázquez,et al.  Protein-only, antimicrobial peptide-containing recombinant nanoparticles with inherent built-in antibacterial activity. , 2017, Acta biomaterialia.

[17]  C. Dobson,et al.  Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. , 2017, Annual review of biochemistry.

[18]  M. Jensen,et al.  Tuning of recombinant protein expression in Escherichia coli by manipulating transcription, translation initiation rates and incorporation of non-canonical amino acids , 2017, bioRxiv.

[19]  E. Vázquez,et al.  Engineering tumor cell targeting in nanoscale amyloidal materials , 2017, Nanotechnology.

[20]  E. Vázquez,et al.  Functional inclusion bodies produced in the yeast Pichia pastoris , 2016, Microbial Cell Factories.

[21]  Zhanglin Lin,et al.  Recombinant production of medium- to large-sized peptides in Escherichia coli using a cleavable self-aggregating tag , 2016, Microbial Cell Factories.

[22]  Pierre Tufféry,et al.  PEP-FOLD3: faster de novo structure prediction for linear peptides in solution and in complex , 2016, Nucleic Acids Res..

[23]  Esther Vázquez,et al.  Conformational and functional variants of CD44-targeted protein nanoparticles bio-produced in bacteria , 2016, Biofabrication.

[24]  Xianpu Ni,et al.  Assembly of a novel biosynthetic pathway for gentamicin B production in Micromonospora echinospora , 2016, Microbial Cell Factories.

[25]  Cui-juan Gao,et al.  Secretory production of antimicrobial peptides in Escherichia coli using the catalytic domain of a cellulase as fusion partner. , 2015, Journal of biotechnology.

[26]  Michael H. Schwartz,et al.  Reversible, Specific, Active Aggregates of Endogenous Proteins Assemble upon Heat Stress , 2015, Cell.

[27]  Zhanglin Lin,et al.  Formation of active inclusion bodies induced by hydrophobic self-assembling peptide GFIL8 , 2015, Microbial Cell Factories.

[28]  N. Ferrer-Miralles,et al.  A novel bio-functional material based on mammalian cell aggresomes , 2015, Applied Microbiology and Biotechnology.

[29]  Vaibhav Upadhyay,et al.  Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process , 2015, Microbial Cell Factories.

[30]  P. Derreumaux,et al.  Improved PEP-FOLD Approach for Peptide and Miniprotein Structure Prediction. , 2014, Journal of chemical theory and computation.

[31]  Germán L. Rosano,et al.  Recombinant protein expression in Escherichia coli: advances and challenges , 2014, Front. Microbiol..

[32]  D. Craik,et al.  Design and characterization of novel antimicrobial peptides, R-BP100 and RW-BP100, with activity against Gram-negative and Gram-positive bacteria. , 2013, Biochimica et biophysica acta.

[33]  Stavros J. Hamodrakas,et al.  A Consensus Method for the Prediction of ‘Aggregation-Prone’ Peptides in Globular Proteins , 2013, PloS one.

[34]  Pierre Tufféry,et al.  PEP-FOLD: an updated de novo structure prediction server for both linear and disulfide bonded cyclic peptides , 2012, Nucleic Acids Res..

[35]  U. Rinas,et al.  Functional Inclusion Bodies Produced in Bacteria as Naturally Occurring Nanopills for Advanced Cell Therapies , 2012, Advanced materials.

[36]  F. Hartl,et al.  DnaK functions as a central hub in the E. coli chaperone network. , 2012, Cell reports.

[37]  P. Dannies Prolactin and growth hormone aggregates in secretory granules: the need to understand the structure of the aggregate. , 2012, Endocrine reviews.

[38]  Zhanglin Lin,et al.  Small surfactant-like peptides can drive soluble proteins into active aggregates , 2012, Microbial Cell Factories.

[39]  S. Singh,et al.  Impact of product-related factors on immunogenicity of biotherapeutics. , 2011, Journal of pharmaceutical sciences.

[40]  William C Wimley,et al.  Describing the mechanism of antimicrobial peptide action with the interfacial activity model. , 2010, ACS chemical biology.

[41]  Yibing Huang,et al.  Alpha-helical cationic antimicrobial peptides: relationships of structure and function , 2010, Protein & Cell.

[42]  N. Ferrer-Miralles,et al.  Rehosting of Bacterial Chaperones for High-Quality Protein Production , 2009, Applied and Environmental Microbiology.

[43]  Vladka Gaberc-Porekar,et al.  Engineering inclusion bodies for non denaturing extraction of functional proteins , 2008, Microbial cell factories.

[44]  F. Avilés,et al.  Inclusion bodies: specificity in their aggregation process and amyloid-like structure. , 2008, Biochimica et biophysica acta.

[45]  Shih-Bin Lin,et al.  Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp. , 2008, International journal of antimicrobial agents.

[46]  Bernd Nidetzky,et al.  Fusion to a pull‐down domain: a novel approach of producing Trigonopsis variabilisD‐amino acid oxidase as insoluble enzyme aggregates , 2007, Biotechnology and bioengineering.

[47]  X. Daura,et al.  AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides , 2007, BMC Bioinformatics.

[48]  S. Withers,et al.  Direct Demonstration of the Flexibility of the Glycosylated Proline-Threonine Linker in the Cellulomonas fimi Xylanase Cex through NMR Spectroscopic Analysis* , 2007, Journal of Biological Chemistry.

[49]  J. Betton,et al.  Formation of active inclusion bodies in the periplasm of Escherichia coli , 2006, Molecular microbiology.

[50]  A. Villaverde,et al.  Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins , 2005, Microbial cell factories.

[51]  E. Romanowski,et al.  A Review of Antimicrobial Peptides and Their Therapeutic Potential as Anti-Infective Drugs , 2005, Current eye research.

[52]  J. Corchero Eukaryotic aggresomes: from a model of conformational diseases to an emerging type of immobilized biocatalyzers , 2015, Applied Microbiology and Biotechnology.

[53]  Hilde van der Togt,et al.  Publisher's Note , 2003, J. Netw. Comput. Appl..