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Poröser Polymorph: Der poröse Polymorph von Guanidinium‐1,4‐benzoldisulfonat (G₂BDS), eines der einfachsten Mitglieder einer archetypischen Klasse wasserstoffverbrückter Gerüste, wurde aus seinem Acetonsolvat durch Einkristall‐zu‐Einkristall (SC‐SC)‐Desolvatisierung hergestellt. Die persistente Porosität, das Phasenverhalten und die Gassorption werden beschrieben.

Abstract

Guanidinium organosulfonates (GSs) are a large and well‐explored archetypal family of hydrogen‐bonded organic host frameworks that have, over the past 25 years, been regarded as nonporous. Reported here is the only example to date of a conventionally microporous GS host phase, namely guanidinium 1,4‐benzenedisulfonate ( p ‐G₂BDS). p ‐G₂BDS is obtained from its acetone solvate, AcMe@G₂BDS, by single‐crystal‐to‐single‐crystal (SC‐SC) desolvation, and exhibits a Type I low‐temperature/pressure N₂ sorption isotherm (SA_BET=408.7(2) m² g⁻¹, 77 K). SC‐SC sorption of N₂, CO₂, Xe, and AcMe by p ‐G₂BDS is explored under various conditions and X‐ray diffraction provides a measurement of the high‐pressure, room temperature Xe and CO₂ sorption isotherms. Though p ‐G₂BDS is formally metastable relative to the “collapsed”, nonporous polymorph, np ‐G₂BDS, a sample of p ‐G₂BDS survived for almost two decades under ambient conditions. np ‐G₂BDS reverts to zCO₂@ p ‐G₂BDS or yXe@ p ‐G₂BDS (y,z=variable) when pressure of CO₂ or Xe, respectively, is applied.

Short linear peptides can overcome certain limitations of small molecules for targeting protein‐protein interactions. Here, the interaction between the human chemokine CCL19 with chemokine receptor CCR7 was investigated to obtain receptor‐derived CCL19‐binding peptides. After identifying a linear binding site of CCR7, five hexapeptides binding to CCL19 in the low micromolar to nanomolar range were designed, guided by pharmacophore and lipophilicity screening of computationally generated peptide libraries. These results corroborate the applicability of the computational approach and the chosen selection criteria to obtain short linear peptides mimicking a protein‐protein interaction site.