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The attachment of a metal complex to amyloid recognition units typically leads to a decrease in peptide affinity. We show here that by separating a macrocyclic GdL chelate and a PiB targeting unit with a long hydrophobic C10 linker, it is possible to attain nanomolar affinities for both A\u03b2<jats:sub>1\u201040<\/jats:sub> (<jats:italic>K<\/jats:italic><jats:sub>d<\/jats:sub>=4.4\u2005n<jats:sc>m<\/jats:sc>) and amylin (<jats:italic>K<\/jats:italic><jats:sub>d<\/jats:sub>=4.5\u2005n<jats:sc>m<\/jats:sc>), implicated, respectively in Alzheimer's disease and diabetes. The Scatchard analysis of surface plasmon resonance data obtained for a series of amphiphilic, PiB derivative GdL complexes indicate that their A\u03b2<jats:sub>1\u201040<\/jats:sub> or amylin binding affinity varies with their concentration, thus micellar aggregation state. The GdL chelates also affect peptide aggregation kinetics, as probed by thioflavin\u2010T fluorescence assays. A 2D NMR study allowed identifying that the hydrophilic region of A\u03b2<jats:sub>1\u201040<\/jats:sub> is involved in the interaction between the monomer peptide and the Gd<jats:sup>3+<\/jats:sup> complex. Finally, ex vivo biodistribution experiments were conducted in healthy mice by using <jats:sup>111<\/jats:sup>In labeled analogues. Their pancreatic uptake, \u223c3\u2009%ID\u2009g<jats:sup>\u22121<\/jats:sup>, is promising to envisage amylin imaging in diabetic animals.<\/jats:p>","DOI":"10.1002\/chem.202004000","type":"journal-article","created":{"date-parts":[[2020,10,7]],"date-time":"2020-10-07T13:59:53Z","timestamp":1602079193000},"page":"2009-2020","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Concentration\u2010Dependent Interactions of Amphiphilic PiB Derivative Metal Complexes with Amyloid Peptides A\u03b2 and Amylin**"],"prefix":"10.1002","volume":"27","author":[{"given":"Saida","family":"Majdoub","sequence":"first","affiliation":[{"name":"Centre de Biophysique Mol\u00e9culaire CNRS UPR 4301 Universit\u00e9 d'Orl\u00e9ans  rue Charles Sadron 45071 Orl\u00e9ans France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Zolt\u00e1n","family":"Garda","sequence":"additional","affiliation":[{"name":"Department of Physical Chemistry Faculty of Science and Technology University of Debrecen  Egyetem t\u00e9r 1 4032 Debrecen Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alexandre C.","family":"Oliveira","sequence":"additional","affiliation":[{"name":"Department of Chemistry University of Coimbra  Coimbra Chemistry Centre (CQC) 3004-535 Coimbra Portugal"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Inga","family":"Relich","sequence":"additional","affiliation":[{"name":"LCC-CNRS Universit\u00e9 de Toulouse, CNRS  Toulouse France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Agn\u00e8s","family":"Pallier","sequence":"additional","affiliation":[{"name":"Centre de Biophysique Mol\u00e9culaire CNRS UPR 4301 Universit\u00e9 d'Orl\u00e9ans  rue Charles Sadron 45071 Orl\u00e9ans France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3865-4379","authenticated-orcid":false,"given":"Sara","family":"Lacerda","sequence":"additional","affiliation":[{"name":"Centre de Biophysique Mol\u00e9culaire CNRS UPR 4301 Universit\u00e9 d'Orl\u00e9ans  rue Charles Sadron 45071 Orl\u00e9ans France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christelle","family":"Hureau","sequence":"additional","affiliation":[{"name":"LCC-CNRS Universit\u00e9 de Toulouse, CNRS  Toulouse France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Carlos F. 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