18 luglio 2022

Spartacus ► L'armamento della biotecnologia (5/7)

"Il progresso non regolamentato delle biotecnologie sta creando una nuova corsa agli armamenti e minaccia la nostra autonomia personale".  Spartacus

Un documento pubblicato online con il nome di "Spartacus" è diventato virale nel 2021. La "lettera di Covid" riassumeva lo stato della "pandemia" in quel momento, mettendo in discussione la cosiddetta "scienza" attribuita al Covid-19 e ai vaccini. Da allora, Spartacus ha scritto diversi documenti, tra cui "Covid-19: A Web of Corruption" e una serie in quattro parti Covid-19: Deep Dive.

Di seguito riportiamo l'ultimo articolo pubblicato da Spartacus, The Weaponization of Biotech:
"Dopo il nostro precedente articolo su questo tema, qualcuno fuori sede mi ha chiesto di citare esempi specifici di biotecnologie che potrebbero essere usate in modo improprio per scopi nefasti, o che potrebbero essere utili come strumenti militari o di intelligence clandestini. Era una critica giusta. Ho elencato una serie di tecnologie che potrebbero avere tali utilizzi, ma non ho citato alcun articolo specifico per sostenere la mia tesi. Questo articolo colmerà questa lacuna".
Pubblichiamo questo documento di Spartacus in sezioni per coloro che hanno difficoltà a trovare il tempo di leggerlo per intero in una sola seduta. Questo è il primo della nostra serie.

Biofabbricazione in vivo

Con alcuni nuovi tipi di biotecnologie, potrebbe essere possibile "stampare" nuove strutture all'interno del corpo utilizzando processi biologici.

Prendiamo ad esempio la ricerca di Ehud Gazit sull'uso di unità amiloidi ripetute per assemblare strutture artificiali.
Le nanostrutture peptidiche e proteiche amiloidi autoassemblate sono state tradizionalmente considerate solo come aggregati patologici implicati nelle malattie neurodegenerative umane. In tempi più recenti, queste nanostrutture hanno trovato interessanti applicazioni come materiali avanzati nella biomedicina, nell'ingegneria dei tessuti, nelle energie rinnovabili, nelle scienze ambientali, nelle nanotecnologie e nella scienza dei materiali, per citare solo alcuni campi. In tutte queste applicazioni, la funzione finale dipende da: (i) dai meccanismi specifici di aggregazione delle proteine, (ii) dalla struttura gerarchica degli amiloidi proteici e peptidici, dalla scala di lunghezza atomistica a quella mesoscopica e (iii) dalle proprietà fisiche degli amiloidi nel contesto dell'ambiente circostante (biologico o artificiale). In questa rassegna, discuteremo i recenti progressi compiuti nel campo degli amiloidi funzionali e artificiali e metteremo in evidenza le connessioni tra i meccanismi di ripiegamento, dispiegamento e aggregazione delle proteine/peptidi, con la struttura e la funzionalità dell'amiloide risultante. Si evidenziano inoltre gli attuali progressi nella progettazione e nella sintesi di materiali biologici e funzionali a base di amiloidi e si identificano nuovi potenziali campi in cui le strutture a base di amiloidi promettono nuove scoperte.
...
In un altro esempio, è stata osservata la formazione di fibrille (le cosiddette nanofibre proteiche) da parte della fibronectina, proteina di adesione della matrice extracellulare (ECM), dopo incubazione a 37 °C in miscele di acqua/etanolo.94 Le fibrille sono state utilizzate come impalcature per depositare punti quantici (QD) a guscio centrale di CdSe-ZnS modificati con N-idrossisolfosuccinimmide (NHS), con potenziali applicazioni come materiali nanoibridi biofotonici. Anche il fibrinogeno forma fibrille con l'incubazione a pH 2 e queste sono state utilizzate come modelli per la biomineralizzazione.95
Studi recenti hanno rivelato che diversi aggregati proteici naturali possiedono proprietà ottiche semiconduttive intrinseche (15). Kaminski et al. hanno dimostrato che, se eccitati a 405 nm, gli assemblaggi di proteine mal ripiegate associate a disturbi neurodegenerativi possono mostrare un'emissione fluorescente intrinseca (16, 17). Questa autofluorescenza priva di etichetta consente di valutare quantitativamente la cinetica delle formazioni fibrillari amiloidi, eliminando la necessità di un'etichettatura estrinseca, che potrebbe causare ostacoli sterici e altre perturbazioni durante l'aggregazione (16).

Le strutture auto-assemblate fatte di peptidi molto corti, compresi i frammenti di tali proteine amiloidogeniche, possono anche avere intriganti proprietà semiconduttive perché le loro lacune di banda sono paragonabili a quelle dei materiali convenzionali (18). Inoltre, la loro natura bioderivata e l'autoassemblaggio rigido (19, 20) possono ridurre al minimo la potenziale citotossicità dei blocchi di costruzione (21), dimostrando la biocompatibilità delle strutture supramolecolari. Gli enantiomeri determinano la sensibilità (di tipo l) o la resistenza (di tipo d) enzimatica delle auto-assemblaggi (22), il che è alla base della loro controllabile biosostenibilità. Inoltre, la debole riducibilità degli amminoacidi implica una forte stabilità all'ossidazione delle strutture supramolecolari (23). In virtù della loro sintesi semplice e a basso costo, nonché della facilità di modulazione rispetto alle loro controparti più grandi, questi semiconduttori peptidici auto-assemblati possono servire come candidati per nanostrutture funzionali interdisciplinari avanzate (24, 25).
Se si potessero assemblare semiconduttori di amiloide nel corpo delle persone in modo ordinato e regolato, si potrebbero assemblare i componenti di un vero e proprio biocomputer all'interno del corpo di una persona.

È una strana coincidenza che le proteine del SARS-CoV-2 siano altamente amiloidogeniche.


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