M. Dolors Ludevid

Center for Research in Agricultural Genomics

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Margarita Torrent

Center for Research in Agricultural Genomics

Ernest Giralt

Universitat de Barcelona

Fernando Alberício

Biomedical Research Networking Center in Bioengineering, Biomaterials and Nanomedicine

Montserrat Pagès

Center for Research in Agricultural Genomics

Pere Puigdomènech

Center for Research in Agricultural Genomics

Immaculada Llop-Tous

Center for Research in Agricultural Genomics

Adela Goday

Center for Research in Agricultural Genomics

Jordi Gómez

Colorado State University

Luis Ruíz-Ávila

Icahn School of Medicine at Mount Sinai

Miriam Bastida

SOM Biotech (Spain)

Cooperative Institutions

Consejo Superior de Investigaciones Científicas

Centro de Investigación y Desarrollo

Centre d’Investigació i Desenvolupament

Universitat de Barcelona

Institut de Biologia Molecular de Barcelona

Center for Research in Agricultural Genomics

Universitat Autònoma de Barcelona

Institute for Research in Biomedicine

FC Barcelona

Centre National de la Recherche Scientifique

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Differential Protein Accumulation in Banana Fruit during Ripening

PLANT PHYSIOLOGY (1992)

Eva Domı́nguez-Puigjaner M. Vendrell M. Dolors Ludevid

Banana (Musa acuminata, cv Dwarf Cavendish) proteins were extracted from pulp tissue at different stages of ripening and analyzed by two-dimensional electrophoresis. The results provide evidence of differential protein accumulation during ripening. Two sets of polypeptides have been detected that increase substantially in ripe fruit. These polypeptides were characterized as glycoproteins by western blotting and concanavalin A binding assays. Antibodies againts tomato polygalacturonase cross-react with one of these sets of proteins.

Musaceae

Musa acuminata

10.1104/pp.98.1.157

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Citations (55)

Two-dimensional gel electrophoresis of zein proteins from normal and opaque-2 maize with non-ionic detergent acid urea-polyacrylamide gel electrophoresis in the first dimension

Plant Science Letters (1984)

JoséA. Martínez Izquierdo M. Dolors Ludevid Pere Puigdomènech Jaume Palau

Sodium dodecyl sulfate

Molecular-weight size marker

Polyacrylamide

10.1016/0304-4211(84)90125-1

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Acid-base properties of 4-nitro-l-histidine and related compounds

Bioorganic Chemistry (1979)

Ernest Giralt M. Dolors Ludevid Fernando Alberício M. Bassedas

Base (topology)

10.1016/0045-2068(79)90037-3

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Citations (3)

Convergent Synthesis of Repeating Peptides (Val-X-Leu-Pro-Pro-Pro)₈Adopting a Polyproline II Conformation

The Journal of Organic Chemistry (1996)

Ionara I. Dalcol Miquel Pons M. Dolors Ludevid Ernest Giralt

The N-terminal domain of maize gamma-zein has a repetitive structure (Val-His-Leu-Pro-Pro-Pro)(8) that has recently been shown to adopt an amphipathic polyproline II type conformation in aqueous solution. We report here the synthesis and conformational analysis of three model peptides (Val-X-Leu-Pro-Pro-Pro)(8) (X = Ala (1), Glu (2), Lys (3)). The three compounds have been synthesized in a very efficient way using a convergent solid-phase strategy. Circular dichroism shows unequivocally that the three model peptides adopt polyproline II (PPII) type conformations under a variety of experimental conditions and that neither the presence of histidine nor amphipathicity of the peptide is an absolute requirement for adopting the native conformation. These results open the door for the de novo design of compounds with PPII conformations and must be taken into account in the structure prediction of protein structures from sequence data banks.

Polyproline helix

Oligopeptide

Sequence (biology)

10.1021/jo960987g

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Citations (30)

D‐SAP: A New, Noncytotoxic, and Fully Protease Resistant Cell‐Penetrating Peptide

ChemMedChem (2007)

Sílvia Pujals Jimena Fernández‐Carneado M. Dolors Ludevid Ernest Giralt

Abstract Protease resistant cell‐penetrating peptides (CPPs) are promising carriers for drugs unable to cross the cell membrane. As these CPPs are stable in vivo for much longer periods of time compared to other classes of therapeutic peptides, noncytotoxicity is a property sine qua non for their pharmacological development. Described herein is a fully protease resistant CPP that is noncytotoxic at concentrations up to 1 m M . Proteolytic stability was obtained by chiral inversion of the residues of a known self‐assembling CPP—from all L ‐amino acids to all D ‐amino acids—and then assessed against trypsin and human serum. Circular dichroism studies confirmed the enantiomeric structure of the analogue, and transmission electron microscopy (TEM) studies indicated that the new inverso analogue retains the ability of the original peptide to self‐assemble. The results of uptake experiments indicate that the protease‐stable (that is, D ‐amino acid) analogue of the peptide is internalised by cells to the same extent as the protease‐susceptible (that is, L ‐amino acid) parent peptide. Also reported herein are the results of studies on the cellular internalisation mechanism of the all‐ D analogue, which reveal the steps followed by the peptide upon its entry into the cell.

Cell-penetrating peptide

10.1002/cmdc.200700267

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Citations (53)

Expression of genes for cell-wall proteins in dividing and wounded tissues ofZea mays L.

Planta (1990)

M. Dolors Ludevid Luis Ruíz-Ávila M. P. Vallés Virginia Stiefel Margarita Torrent

Coleoptile

Elongation

10.1007/bf02411450

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Citations (58)