Fluorescence analysis of matrix functionalization.

<p>A) Emission spectrum (λ_exc 380 nm) of 5 mM <i>p</i>-ACA in 0.4 M NaHCO₃, 1 M NaCl (pH 8,3). B) Emission spectra (λ_exc 350 nm) of suspensions of <i>p</i>-ACA/matrix (50 μl, drained volume; solid line) and EA/matrix (50 μl, drained volume; dashed line) in 2 mL of 0.4 M NaHCO₃, 1 M NaCl (pH 8,3). A. U., arbitrary units.</p

Global anti-biofilm performance of ZA-related compounds and structures with the most significant anti-biofilm performance.

<p>Global anti-biofilm performance value of each ZA-related compound calculated as (sum of cell adhesion codes of all concentrations)-(sum of planktonic growth codes of all concentrations). Values equal to 0 were considered without anti-biofilm performance, below 0 were considered globally able to exert an anti-biofilm activity, and above 0 were considered able to improve biofilm performance. Yellow: no anti-biofilm performance; Light orange: little anti-biofilm performance; Medium orange: moderate anti-biofilm performace; Dark orange: optimal anti-biofilm performance; Light green: little improvement of anti-biofilm performance; Medium green: moderate improvement of anti-biofilm performance; Dark green: optimal improvement of anti-biofilm performance.</p

Structures of cinnamic acid analogues used in the present study.

<p>Structures of cinnamic acid analogues used in the present study.</p

Synthetic scheme of compounds 23, 24, 33, 34, 35, 38.

<p>Reagents and conditions: i) from <b>1</b> for <b>23</b>, from <b>5</b> for <b>24</b>, from <b>32</b> for <b>33</b>: H₂SO₄, MeOH, reflux, 1 h; ii) from <b>32</b>: Py · SO₃, DMF dry, 120°C, 25 min; iii) CH₃I, anhydrous K₂CO₃, dry DMF, reflux, 1.5 h; iv) 1N NaOH, EtOH.</p

Synthetic scheme of compounds 36, 37.

<p>Reagents and conditions: i) Lindlar catalyst, H₂, pyridine, MeOH, r.t., 16 h; ii) 1N NaOH, EtOH/THF (1:1), r.t., 12 h.</p

Structural formula of zosteric acid (ZA) and cinnamic acid (4).

<p>Structural formula of zosteric acid (ZA) and cinnamic acid (4).</p

Mass spectrometry analysis of hydrolyzed <i>p</i>-ACA/matrix.

<p>The eXtracted Ion Current (XIC) profile at 164.069 <i>m/z</i>, recorded during the LC-MS run, is shown. LC retention time on main peak is evidenced. The 164.069 <i>m/z</i> ion corresponds (ΔM = 0.002 Da) to the theoretical <i>m/z</i> value of the [M+H]⁺ of <i>p</i>-ACA. NL: normalization level.</p

Synthetic scheme of compounds 23, 24, 33, 34, 35, 38.

<p>Reagents and conditions: i) from <b>1</b> for <b>23</b>, from <b>5</b> for <b>24</b>, from <b>32</b> for <b>33</b>: H₂SO₄, MeOH, reflux, 1 h; ii) from <b>32</b>: Py · SO₃, DMF dry, 120°C, 25 min; iii) CH₃I, anhydrous K₂CO₃, dry DMF, reflux, 1.5 h; iv) 1N NaOH, EtOH.</p

Mass spectrometry protein identification.

<p>Mass spectrometry protein identification.</p

Synthetic scheme of compounds 2, 7, 8, 11, 17.

<p>Reagents and conditions: i) malonic acid, Py, piperidine, reflux, 80–180 min.</p