Sodium chloride (nacl)

1,2-Dipalmitoyl-sn-glycero-3-phosphocholine (DPPC, Lot. 160PC-318), sphingomyelin egg chicken (SM, Lot. 860061P-25MG-A-116), 1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine (DPPE, Lot. 160PE-106), 1,2-dipalmitoyl-sn-glycero-3-phospho-L-serine sodium salt (DPPS, Lot. 840037P-500MG-A-078CL750332P-200MG-A-030), 1-palmitoyl-2-oleoyl-glycero-3-phosphocholine (POPC, Lot. 850457P-500MG-A-211), 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (POPE, Lot. 850757P-500MG-B-151), and 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-L-serine sodium salt (POPS, Lot. 840034P-25MG-A-250) were purchased from Avanti Polar Lipids (Alabaster, AL, USA). HEPES was purchased from Sigma-Aldrich (St. Louis, MO, USA), NaCl from Carlo Erba (Val-de-Reuil, Normandy, France), and EDTA from Amresco (Solon, OH, USA).
LTX-315 peptide (KKWWKKWDipK-NH₂) Dip: diphenylalanine (Lot. U037QFC180-14/PE6102) was synthesized according to the sequence by solid-phase methods and purchased from GenScript (Piscataway Township, NJ, USA). The purity of the peptide was determined to be higher than 95% by analytical HPLC, TFA removal was performed, and the molecular weight was confirmed with MALDI-TOF mass spectrometry (Figure S1).

Ingredients for media were purchased from Himedia Laboratories (Mumbai, India).
Czapek Yeast Agar (CYA, [69 ]), supplemented with sodium chloride (NaCl) (Carlo Erba, Milan, Italy) to modify the original a_w = 0.99, was used to perform the ecological trials (Table 6).

The bacterial strain Escherichia coli K12-MG1655 (ATCC 700926; genotype, F-lambda-ilvG-rfb-50 rph-1) was used as a model organism. Bacteria were cultivated according to Bittel et al. [29 (link)]. Luria-Bertani (LB) medium was used, which was prepared as follows: 1 L of distilled water was supplemented with 10 g tryptone (Biokar Diagnostics, Allonne, France, ref A1401HA), 5 g yeast extract (Biokar Diagnostics, ref A1202HA) and 5 g NaCl (Carlo Erba Reagents, Milan, Italy, ref 479687). Sterilization was performed by autoclaving at 120 ${}^{\circ }$ C for 20 min. Starting from 10 mL overnight precultures, 50 mL cultures were generated with an optical density ( $O{D}_{620nm}$ ) of = 0.1, with both cultures shaken at 250 rpm at 30 ${}^{\circ }$ C (Eppendorf Innova^® 42 Benchtop incubator shaker, Eppendorf, France). Growth was monitored over time on bacterial culture diluted 1/10 in LB media measured by a spectrophotometer (SAFAS UVmc2) at 620 nm in disposable cuvettes (Brand GmBH, ref 759015) until it reached $O{D}_{620nm}$ = 0.4, which corresponds to the middle of the exponential growth phase.

All the solvents used for hydrocarbon preparation, spiking, and extraction from soil (dichloromethane, methanol, and toluene) were analytical grade and provided by Sigma-Aldrich. Heavy crude oil and asphaltene samples (molecular composition of C: 84%; H: 8%; N: 1.5%; S: 4.5%; O: 1.5%; H/C ratio: 1.14; Ni: 406 mg kg⁻¹, V: 1601 mg kg⁻¹, MW: 2000 Da) were provided by the Colombian Institute of Petroleum. M9 minimal medium used for microbial isolation was composed of Na₂HPO₄, 12.8 g l⁻¹; KH₂PO₄, 3 g l⁻¹; NH₄Cl, 1 g l⁻¹; CaCl₂.2H₂O, 0.015 g l⁻¹; FeSO₄.6H₂O, 0.01 g l⁻¹ (Sigma-Aldrich); NaCl, 0.5 g l⁻¹; and MgSO₄.7H₂O, 1 g l⁻¹ (Carlo Erba Reagents) (Cold Spring Harbor Laboratory 2010 ). Starch casein agar (SCA) was composed of starch, 10 g l⁻¹; casein, 0.3 g l⁻¹ (Scharlau); KH₂PO₄, 2 g l⁻¹; NH₄Cl, 2 g l⁻¹; FeSO₄.6H₂O, 0.05 g l⁻¹; FeSO₄.6H₂O, 0.01 g l⁻¹; and bacteriological agar, 15 g l⁻¹ (Sigma-Aldrich) (Kuster and Williams 1964 (link)). Brain heart infusion (BHI) broth was composed of brain heart infusion, 17.5 g l⁻¹; proteose peptone, 10 g l⁻¹; NaCl, 5 g l⁻¹; Na₂HPO₄, 2 g l⁻¹; and dextrose, 2 g l⁻¹ (PanReac AppliChem).

Cells were centrifuged at 1000× g for 10 min. The pellets were washed 2× with RPMI 1640 modified medium, centrifuged again at 1000× g for 10 min, resuspended in 0.1 M Tris–HCl (Carlo Erba, Milan, Italy) at pH 7.2, and used in part for homogenate analysis and in part for nuclei purification. The homogenate was then used for biochemical determinations and for evaluation of ³H-Dex radioactivity. Nuclei were isolated as previously reported [38 (link)] and checked for possible cytoplasmic contamination as previously reported [39 (link)]. The NLM were prepared in sucrose gradient and checked for possible contamination according to Cascianelli et al. [22 (link)]. The extraction was carried out with Triton X-100 (Sigma Aldrich Co., St. Louis, MO, USA) dissolved in distilled water (10% v/v), on ice, added to the purified nuclei to a final detergent concentration of 1% (v/v).The extract was placed in a cushion of 80% sucrose with a gradient of 15%–40% sucrose on top. After centrifugation overnight, floating fractions corresponding to 3 mL were carefully collected with a pipette, diluted five times with 25 mM HEPES–HCl (Carlo Erba, Milan, Italy), 150 mM NaCl, (Carlo Erba, Milan, Italy) pH 7.1 and centrifuged at 100,000× g for 120 min.