Alessandro Lobbia

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Trends

Author Order

Document Type

Co-Authors

Johann Mulzer

University of Vienna

Peter Luger

Freie Universität Berlin

J. Buschmann

Freie Universität Berlin

Fridtjof Schröder

Givaudan (Switzerland)

Jean Pierre Bali

Université de Montpellier

Luis Moroder

Max Planck Institute of Biochemistry

Gianfranco Borin

Ospedale Sacro Cuore Don Calabria

Wolfram Saenger

Freie Universität Berlin

Erich Wünsch

Czech Academy of Sciences

AE Oakley

North Tyneside General Hospital

Cooperative Institutions

Freie Universität Berlin

Max Planck Institute of Biochemistry

Goethe University Frankfurt

Technische Universität Berlin

Max Planck Society

Yale University

Max Planck Institute for Molecular Genetics

München Klinik

Heidelberg University

Centre National de la Recherche Scientifique

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Field

Aggregation of Aβ Alzheimer's disease‐related peptide studied by dynamic light scattering

Journal of Peptide Research (1998)

Markus Thunecke Alessandro Lobbia Ulrich Kosciessa Thomas Dyrks AE Oakley

The aggregation behavior of the major component of Alzheimer's disease-related, amyloid peptides, Abeta-(1-40) and Abeta-(1-42), was studied in solution using dynamic light scattering. With most solvents employed, we found fibrils coexisting with oligomeric Abeta species. Pronounced differences were observed in aggregation of Abeta-(1-40) and (1-42) sequences in acetonitrile-water mixtures. Cofactors such as Zn2+ were found to induce deaggregation of Abeta instead of aggregation. The results indicated that the initial state of the peptide immediately after synthesis is rather poorly defined. Using freezing instead of lyophilization after the final peptide synthesis step, may partially relieve these problems.

10.1111/j.1399-3011.1998.tb01255.x

Cite

Citations (22)

Synthese einer neuen nichtnatürlichen Aminosäure mit einem Benzodiazepinrest in der Seitenkette und Einbau in ein Tripeptid

Angewandte Chemie (1994)

Johann Mulzer Fridtjof Schröder Alessandro Lobbia J. Buschmann Peter Luger

Peptidmimetica auf der Grundlage von Benzodiazepinen werden mit nichtnatürlichen Aminosäuren wie 1 zugänglich. Sie können als peptidische und wegen der modifizierten Aminosäureseitenkette auch als nichtpeptidische Rezeptorliganden fungieren. 1 wurde in sieben Stufen und 15% Gesamtausbeute aus L ‐Glutaminsäuremonomethylester hergestellt. magnified image

10.1002/ange.19941061710

Cite

Citations (8)

Structure-Function Studies on Gastrin Related Peptides

De Gruyter eBooks (1984)

Luis Moroder Gianfranco Borin Alessandro Lobbia Jean Pierre Bali Eva‐Maria Wunsch

Gastrin-releasing peptide

10.1515/9783112315972-035

Cite

Citations (0)

ChemInform Abstract: Synthesis of a New Unnatural Amino Acid with a Benzodiazepine- Containing Side Chain and Incorporation into a Tripeptide.

ChemInform (1995)

Johann Mulzer Frank C. Schroeder Alessandro Lobbia J. Buschmann Peter Luger

Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.

Tripeptide

Side chain

10.1002/chin.199506224

Cite

Citations (0)

Synthese von Gastrin-aktiven Peptiden. Untersuchungen zur Struktur-Wirkungsbeziehung des natürlichen Hormons Human-Little-Gastrin-I

Hoppe-Seyler´s Zeitschrift für physiologische Chemie (1984)

Walter Göhring Luis Moroder Gianfranco Borin Alessandro Lobbia Jean Pierre Bali

To identify the role of the block of glutamic acid residues characteristic for the gastrin molecule, a series of shortened peptides related to the human little-gastrin-I sequence were synthesized. The biological activities of these gastrin peptides strongly suggest in the pentaglutamic acid sequence a specific information for a pronounced amplification of the hormonal activity.

Sequence (biology)

10.1515/bchm2.1984.365.1.83

Cite

Citations (28)

Synthesis of a New Unnatural Amino Acid with a Benzodiazepine‐Containing Side Chain and Incorporation into a Tripeptide

Angewandte Chemie International Edition (1994)

Johann Mulzer Fridtjof Schröder Alessandro Lobbia J. Buschmann Peter Luger

Peptidomimetics based on benzodiazepines can be made from nonnatural amino acids such as 1. They can function both as peptidic and nonpeptidic receptor ligands, owing to the modified amino acid side chains. Compound 1 was synthesized from monomethyl L-glutamate in seven steps in 15% overall yield.

Side chain

Tripeptide

Peptidomimetic

10.1002/anie.199417371

Cite

Citations (19)